{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T18:30:14Z","timestamp":1790706614636,"version":"4.1.0"},"reference-count":105,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,10,1]],"date-time":"2022-10-01T00:00:00Z","timestamp":1664582400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100006224","name":"Argonne National Laboratory","doi-asserted-by":"publisher","award":["1R15GM123425-01"],"award-info":[{"award-number":["1R15GM123425-01"]}],"id":[{"id":"10.13039\/100006224","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006224","name":"Argonne National Laboratory","doi-asserted-by":"publisher","award":["DE-AC02-06CH11357"],"award-info":[{"award-number":["DE-AC02-06CH11357"]}],"id":[{"id":"10.13039\/100006224","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","award":["R01 GM104257"],"award-info":[{"award-number":["R01 GM104257"]}],"id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["P30 GM124165"],"award-info":[{"award-number":["P30 GM124165"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["S10OD021527"],"award-info":[{"award-number":["S10OD021527"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"NIGMS","doi-asserted-by":"publisher","award":["R01 GM104257"],"award-info":[{"award-number":["R01 GM104257"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"NIGMS","doi-asserted-by":"publisher","award":["1R15GM123425-01"],"award-info":[{"award-number":["1R15GM123425-01"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006132","name":"Office of Science","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006132","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100012005","name":"University of Massachusetts Boston","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012005","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2022,10]]},"DOI":"10.1016\/j.jbc.2022.102454","type":"journal-article","created":{"date-parts":[[2022,9,5]],"date-time":"2022-09-05T13:17:16Z","timestamp":1662383836000},"page":"102454","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"title":["High-resolution structures of a siderophore-producing cyclization domain from Yersinia pestis offer a refined proposal of substrate binding"],"prefix":"10.1016","volume":"298","author":[{"given":"Andrew D.","family":"Gnann","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1435-2264","authenticated-orcid":false,"given":"Yuan","family":"Xia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6159-4354","authenticated-orcid":false,"given":"Jess","family":"Soule","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clara","family":"Barth\u00e9lemy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jayata S.","family":"Mawani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarah Nzikoba","family":"Musoke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian M.","family":"Castellano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward J.","family":"Brignole","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique P.","family":"Frueh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel P.","family":"Dowling","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2022.102454_bib1","doi-asserted-by":"crossref","first-page":"9259","DOI":"10.1073\/pnas.1401734111","article-title":"Atlas of nonribosomal peptide and polyketide biosynthetic pathways reveals common occurrence of nonmodular enzymes","volume":"111","author":"Wang","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102454_bib2","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1038\/s41586-018-0207-y","article-title":"Novel soil bacteria possess diverse genes for secondary metabolite biosynthesis","volume":"558","author":"Crits-Christoph","year":"2018","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102454_bib3","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1039\/b906679a","article-title":"Chemistry and biology of siderophores","volume":"27","author":"Hider","year":"2010","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.jbc.2022.102454_bib4","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1038\/s41589-019-0385-4","article-title":"Pass-back chain extension expands multimodular assembly line biosynthesis","volume":"16","author":"Zhang","year":"2020","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib5","doi-asserted-by":"crossref","first-page":"6841","DOI":"10.1016\/S0040-4039(99)01377-5","article-title":"Agrochelin, a new cytotoxic alkaloid from the marine bacteria Agrobacterium sp","volume":"40","author":"Ca\u00f1edo","year":"1999","journal-title":"Tetrahedron Lett."},{"key":"10.1016\/j.jbc.2022.102454_bib6","doi-asserted-by":"crossref","first-page":"328","DOI":"10.7164\/antibiotics.51.328","article-title":"Micacocidin A, B and C, novel antimycoplasma agents from Pseudomonas sp. II. Structure elucidation","volume":"51","author":"Kobayashi","year":"1998","journal-title":"J.\u00a0Antibiot. (Tokyo)"},{"key":"10.1016\/j.jbc.2022.102454_bib7","first-page":"2325","article-title":"Epothilones, a new class of microtubule-stabilizing agents with a taxol-like mechanism of action","volume":"55","author":"Bollag","year":"1995","journal-title":"Cancer Res."},{"key":"10.1016\/j.jbc.2022.102454_bib8","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1126\/science.102.2650.376","article-title":"Bacitracin: a new antibiotic produced by a member of the B.\u00a0subtilis group","volume":"102","author":"Johnson","year":"1945","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102454_bib9","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1007\/s12257-020-0265-5","article-title":"Recent advances in re-engineering modular PKS and NRPS assembly lines","volume":"25","author":"Beck","year":"2020","journal-title":"Biotechnol. Bioproc. Eng."},{"key":"10.1016\/j.jbc.2022.102454_bib10","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/S1286-4579(01)01412-5","article-title":"The Yersinia high-pathogenicity island: an iron-uptake island","volume":"3","author":"Carniel","year":"2001","journal-title":"Microbes Infect."},{"key":"10.1016\/j.jbc.2022.102454_bib11","doi-asserted-by":"crossref","first-page":"14941","DOI":"10.1021\/bi991787c","article-title":"Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: in\u00a0vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF","volume":"38","author":"Quadri","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib12","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S0021-9258(17)43671-4","article-title":"Vibriobactin, a siderophore from Vibrio cholerae","volume":"259","author":"Griffiths","year":"1984","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102454_bib13","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/S1074-5521(98)90291-5","article-title":"Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin","volume":"5","author":"Quadri","year":"1998","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib14","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/0006-291X(70)90819-3","article-title":"Enterobactin, an iron transport compound from Salmonella typhimurium","volume":"38","author":"Pollack","year":"1970","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jbc.2022.102454_bib15","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1517\/17460441.2012.708335","article-title":"Targeting iron assimilation to develop new antibacterials","volume":"7","author":"Foley","year":"2012","journal-title":"Expert Opin. Drug Discov."},{"key":"10.1016\/j.jbc.2022.102454_bib16","doi-asserted-by":"crossref","first-page":"8518","DOI":"10.1002\/anie.201404977","article-title":"The structure of a transient complex of a nonribosomal peptide synthetase and a cytochrome P450 monooxygenase","volume":"53","author":"Haslinger","year":"2014","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jbc.2022.102454_bib17","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1111\/j.1574-6968.2000.tb09225.x","article-title":"An oxidation domain in the BlmIII non-ribosomal peptide synthetase probably catalyzing thiazole formation in the biosynthesis of the anti-tumor drug bleomycin in Streptomyces verticillus ATCC15003","volume":"189","author":"Du","year":"2000","journal-title":"FEMS Microbiol. Lett."},{"key":"10.1016\/j.jbc.2022.102454_bib18","doi-asserted-by":"crossref","first-page":"9722","DOI":"10.1021\/bi034792w","article-title":"Oxidase domains in epothilone and bleomycin biosynthesis: thiazoline to thiazole oxidation during chain elongation","volume":"42","author":"Schneider","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib19","doi-asserted-by":"crossref","first-page":"15946","DOI":"10.1021\/bi0481139","article-title":"Portability of oxidase domains in nonribosomal peptide synthetase modules","volume":"43","author":"Schneider","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib20","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1186\/1471-2105-9-454","article-title":"In silico analysis of methyltransferase domains involved in biosynthesis of secondary metabolites","volume":"9","author":"Ansari","year":"2008","journal-title":"BMC Bioinform."},{"key":"10.1016\/j.jbc.2022.102454_bib21","doi-asserted-by":"crossref","first-page":"8434","DOI":"10.1021\/ja016398w","article-title":"C-methyltransferase and cyclization domain activity at the intraprotein PK\/NRP switch point of yersiniabactin synthetase","volume":"123","author":"Miller","year":"2001","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102454_bib22","doi-asserted-by":"crossref","first-page":"5802","DOI":"10.1016\/j.jmb.2020.09.004","article-title":"Unimodular methylation by adenylation-thiolation domains containing an embedded methyltransferase","volume":"432","author":"Mori","year":"2020","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib23","doi-asserted-by":"crossref","first-page":"9023","DOI":"10.1021\/bi010519n","article-title":"In\u00a0vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities","volume":"40","author":"Patel","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib24","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1021\/acs.biochem.8b00716","article-title":"Stuffed methyltransferase catalyzes the penultimate step of pyochelin biosynthesis","volume":"58","author":"Ronnebaum","year":"2019","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib25","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1186\/s13036-019-0195-y","article-title":"Modified substrate specificity of a methyltransferase domain by protein insertion into an adenylation domain of the bassianolide synthetase","volume":"13","author":"Xu","year":"2019","journal-title":"J.\u00a0Biol. Eng."},{"key":"10.1016\/j.jbc.2022.102454_bib26","doi-asserted-by":"crossref","first-page":"10082","DOI":"10.1021\/ja0735857","article-title":"Kinetic analysis of teicoplanin glycosyltransferases and acyltransferase reveal ordered tailoring of aglycone scaffold to reconstitute mature teicoplanin","volume":"129","author":"Howard-Jones","year":"2007","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102454_bib27","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1093\/molbev\/msn150","article-title":"Halogenase genes in nonribosomal peptide synthetase gene clusters of Microcystis (cyanobacteria): sporadic distribution and evolution","volume":"25","author":"Cadel-Six","year":"2008","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jbc.2022.102454_bib28","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1016\/j.chembiol.2005.08.010","article-title":"Generation of D amino acid residues in assembly of arthrofactin by dual condensation\/epimerization domains","volume":"12","author":"Balibar","year":"2005","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib29","doi-asserted-by":"crossref","first-page":"10514","DOI":"10.1021\/bi034840c","article-title":"Epimerization of an L-cysteinyl to a D-cysteinyl residue during thiazoline ring formation in siderophore chain elongation by pyochelin synthetase from Pseudomonas aeruginosa","volume":"42","author":"Patel","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib30","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1016\/j.bbapap.2017.05.010","article-title":"Structural and functional aspects of the nonribosomal peptide synthetase condensation domain superfamily: discovery, dissection and diversity","volume":"1865","author":"Bloudoff","year":"2017","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"10.1016\/j.jbc.2022.102454_bib31","doi-asserted-by":"crossref","first-page":"1727","DOI":"10.1002\/jlac.1995199510243","article-title":"Structure elucidation of yersiniabactin, a siderophore from highly virulent Yersinia strains","volume":"1995","author":"Drechsel","year":"1995","journal-title":"Liebigs Annalen"},{"key":"10.1016\/j.jbc.2022.102454_bib32","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1099\/13500872-145-5-1181","article-title":"Yersiniabactin from Yersinia pestis: biochemical characterization of the siderophore and its role in iron transport and regulation","volume":"145","author":"Perry","year":"1999","journal-title":"Microbiology"},{"key":"10.1016\/j.jbc.2022.102454_bib33","doi-asserted-by":"crossref","first-page":"1495","DOI":"10.1016\/j.jinorgbio.2006.04.007","article-title":"Crystal structure of ferric-yersiniabactin, a virulence factor of Yersinia pestis","volume":"100","author":"Miller","year":"2006","journal-title":"J.\u00a0Inorg. Biochem."},{"key":"10.1016\/j.jbc.2022.102454_bib34","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1016\/j.micinf.2011.04.008","article-title":"Yersiniabactin iron uptake: mechanisms and role in Yersinia pestis pathogenesis","volume":"13","author":"Perry","year":"2011","journal-title":"Microbes Infect."},{"key":"10.1016\/j.jbc.2022.102454_bib35","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1111\/j.1365-2958.1993.tb01583.x","article-title":"Virulence of Yersinia enterocolitica is closely associated with siderophore production, expression of an iron-repressible outer membrane polypeptide of 65,000 Da and pesticin sensitivity","volume":"8","author":"Heesemann","year":"1993","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2022.102454_bib36","doi-asserted-by":"crossref","first-page":"4443","DOI":"10.1128\/JB.181.15.4443-4451.1999","article-title":"Iron acquisition and metabolism by mycobacteria","volume":"181","author":"De Voss","year":"1999","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2022.102454_bib37","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1128\/jb.167.1.57-65.1986","article-title":"Characterization of anguibactin, a novel siderophore from Vibrio anguillarum 775(pJM1)","volume":"167","author":"Actis","year":"1986","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2022.102454_bib38","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1128\/IAI.02904-14","article-title":"Blocking yersiniabactin import attenuates extraintestinal pathogenic Escherichia coli in cystitis and pyelonephritis and represents a novel target to prevent urinary tract infection","volume":"83","author":"Brumbaugh","year":"2015","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jbc.2022.102454_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003495","article-title":"Mutated and bacteriophage T4 nanoparticle arrayed F1-V immunogens from Yersinia pestis as next generation plague vaccines","volume":"9","author":"Tao","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2022.102454_bib40","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1021\/acs.chemrev.0c01005","article-title":"Iron acquisition systems of gram-negative bacterial pathogens define TonB-dependent pathways to novel antibiotics","volume":"121","author":"Klebba","year":"2021","journal-title":"Chem. Rev."},{"key":"10.1016\/j.jbc.2022.102454_bib41","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.freeradbiomed.2016.10.489","article-title":"Siderophore-mediated iron acquisition and modulation of host-bacterial interactions","volume":"105","author":"Ellermann","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jbc.2022.102454_bib42","doi-asserted-by":"crossref","first-page":"6743","DOI":"10.1128\/jb.178.23.6743-6751.1996","article-title":"Characterization of a large chromosomal \"high-pathogenicity island\" in biotype 1B Yersinia enterocolitica","volume":"178","author":"Carniel","year":"1996","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2022.102454_bib43","doi-asserted-by":"crossref","first-page":"kuab018","DOI":"10.1093\/jimb\/kuab018","article-title":"Docking domain-mediated subunit interactions in natural product megasynth(et)ases","volume":"48","author":"Smith","year":"2021","journal-title":"J.\u00a0Ind. Microbiol. Biotechnol."},{"key":"10.1016\/j.jbc.2022.102454_bib44","doi-asserted-by":"crossref","first-page":"12432","DOI":"10.1073\/pnas.1608615113","article-title":"Structural elements of an NRPS cyclization domain and its intermodule docking domain","volume":"113","author":"Dowling","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102454_bib45","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1073\/pnas.1614191114","article-title":"Structural and mutational analysis of the nonribosomal peptide synthetase heterocyclization domain provides insight into catalysis","volume":"114","author":"Bloudoff","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102454_bib46","doi-asserted-by":"crossref","first-page":"eabn6549","DOI":"10.1126\/sciadv.abn6549","article-title":"Global protein dynamics as communication sensors in peptide synthetase domains","volume":"8","author":"Mishra","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2022.102454_bib47","doi-asserted-by":"crossref","first-page":"14554","DOI":"10.1002\/anie.202102760","article-title":"Structural and functional analyses of the tridomain-nonribosomal peptide synthetase FmoA3 for 4-methyloxazoline ring formation","volume":"60","author":"Katsuyama","year":"2021","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jbc.2022.102454_bib48","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1038\/s41467-022-28284-x","article-title":"Catalytic trajectory of a dimeric nonribosomal peptide synthetase subunit with an inserted epimerase domain","volume":"13","author":"Wang","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102454_bib49","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1038\/s41557-019-0335-5","article-title":"Structural basis for chain release from the enacyloxin polyketide synthase","volume":"11","author":"Kosol","year":"2019","journal-title":"Nat. Chem."},{"key":"10.1016\/j.jbc.2022.102454_bib50","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib51","doi-asserted-by":"crossref","DOI":"10.1126\/science.aaw4388","article-title":"Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility","volume":"366","author":"Reimer","year":"2019","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102454_bib52","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1038\/nature16163","article-title":"Structures of two distinct conformations of holo-non-ribosomal peptide synthetases","volume":"529","author":"Drake","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102454_bib53","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1002\/cbic.201700030","article-title":"Molecular cross-talk between nonribosomal peptide synthetase carrier proteins and unstructured linker regions","volume":"18","author":"Harden","year":"2017","journal-title":"Chembiochem"},{"key":"10.1016\/j.jbc.2022.102454_bib54","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1021\/ja026939x","article-title":"Haddock: a protein-protein docking approach based on biochemical or biophysical information","volume":"125","author":"Dominguez","year":"2003","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102454_bib55","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1002\/prot.21723","article-title":"HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets","volume":"69","author":"de Vries","year":"2007","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2022.102454_bib56","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1016\/j.jmb.2015.09.014","article-title":"The HADDOCK2.2 web server: user-friendly integrative modeling of biomolecular complexes","volume":"428","author":"van Zundert","year":"2016","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib57","doi-asserted-by":"crossref","first-page":"2511","DOI":"10.1038\/s41467-021-22623-0","article-title":"Structures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity","volume":"12","author":"Izor\u00e9","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102454_bib58","doi-asserted-by":"crossref","first-page":"3432","DOI":"10.1038\/s41467-019-11383-7","article-title":"The structural basis of N-acyl-alpha-amino-beta-lactone formation catalyzed by a nonribosomal peptide synthetase","volume":"10","author":"Kreitler","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2022.102454_bib59","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/j.chembiol.2016.02.012","article-title":"Chemical probes allow structural insight into the condensation reaction of nonribosomal peptide synthetases","volume":"23","author":"Bloudoff","year":"2016","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib60","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1038\/nprot.2015.043","article-title":"The FTMap family of web servers for determining and characterizing ligand-binding hot spots of proteins","volume":"10","author":"Kozakov","year":"2015","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.jbc.2022.102454_bib61","doi-asserted-by":"crossref","first-page":"4729","DOI":"10.1021\/bi992923g","article-title":"Expression, purification, and characterization of HMWP2, a 229 kDa, six domain protein subunit of Yersiniabactin synthetase","volume":"39","author":"Keating","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2022.102454_bib62","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Met. Enzymol."},{"key":"10.1016\/j.jbc.2022.102454_bib63","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib64","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib65","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib66","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1107\/S0021889808006985","article-title":"CHAINSAW: a program for mutating pdb files used as templates in molecular replacement","volume":"41","author":"Stein","year":"2008","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib67","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","author":"Winn","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib68","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib69","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib70","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib71","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2022.102454_bib72","series-title":"Schr\u00f6dinger Release 2020-4: Protein Preparation Wizard","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib73","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s10822-013-9644-8","article-title":"Protein and ligand preparation: parameters, protocols, and influence on virtual screening enrichments","volume":"27","author":"Sastry","year":"2013","journal-title":"J.\u00a0Comput. Aided Mol. Des."},{"key":"10.1016\/j.jbc.2022.102454_bib74","series-title":"Schr\u00f6dinger Release 2020-4","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib75","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1007\/s10822-010-9349-1","article-title":"Towards the comprehensive, rapid, and accurate prediction of the favorable tautomeric states of drug-like molecules in aqueous solution","volume":"24","author":"Greenwood","year":"2010","journal-title":"J.\u00a0Comput. Aided Mol. Des."},{"key":"10.1016\/j.jbc.2022.102454_bib76","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1007\/s10822-007-9133-z","article-title":"Epik: a software program for pK(a) prediction and protonation state generation for drug-like molecules","volume":"21","author":"Shelley","year":"2007","journal-title":"J.\u00a0Comput. Aided Mol. Des."},{"key":"10.1016\/j.jbc.2022.102454_bib77","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1021\/ja00214a001","article-title":"The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin","volume":"110","author":"Jorgensen","year":"1988","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102454_bib78","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1021\/acs.jctc.5b00864","article-title":"OPLS3: a force field providing broad coverage of drug-like small molecules and proteins","volume":"12","author":"Harder","year":"2016","journal-title":"J.\u00a0Chem. Theor. Comput."},{"key":"10.1016\/j.jbc.2022.102454_bib79","doi-asserted-by":"crossref","first-page":"11225","DOI":"10.1021\/ja9621760","article-title":"Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids","volume":"118","author":"Jorgensen","year":"1996","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.jbc.2022.102454_bib80","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1021\/ct900587b","article-title":"Prediction of absolute solvation free energies using molecular dynamics free energy perturbation and the OPLS force field","volume":"6","author":"Shivakumar","year":"2010","journal-title":"J.\u00a0Chem. Theor. Comput."},{"key":"10.1016\/j.jbc.2022.102454_bib81","series-title":"Schr\u00f6dinger Release 2020-4: Prime","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib82","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/S0022-2836(02)00470-9","article-title":"On the role of the crystal environment in determining protein side-chain conformations","volume":"320","author":"Jacobson","year":"2002","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib83","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1002\/prot.10613","article-title":"A\u00a0hierarchical approach to all-atom protein loop prediction","volume":"55","author":"Jacobson","year":"2004","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2022.102454_bib84","doi-asserted-by":"crossref","first-page":"1646","DOI":"10.1002\/prot.24551","article-title":"Antibody structure determination using a combination of homology modeling, energy-based refinement, and loop prediction","volume":"82","author":"Zhu","year":"2014","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2022.102454_bib85","series-title":"Schr\u00f6dinger Release 2020-4: Desmond Molecular Dynamics System, D. E. Shaw Research, New York, NY","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib86","series-title":"Proceedings of the 2006 ACM\/IEEE Conference on Supercomputing","first-page":"84","article-title":"Scalable algorithms for molecular dynamics simulations on commodity clusters","author":"Bowers","year":"2006"},{"key":"10.1016\/j.jbc.2022.102454_bib87","series-title":"Schr\u00f6dinger Release 2020-4","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib88","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.729513","article-title":"Structural biology in the clouds: the WeNMR-EOSC ecosystem","volume":"8","author":"Honorato","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2022.102454_bib89","doi-asserted-by":"crossref","first-page":"1739","DOI":"10.1021\/jm0306430","article-title":"Glide: a new approach for rapid, accurate docking and scoring. 1. method and assessment of docking accuracy","volume":"47","author":"Friesner","year":"2004","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2022.102454_bib90","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1021\/jm030644s","article-title":"Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening","volume":"47","author":"Halgren","year":"2004","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2022.102454_bib91","doi-asserted-by":"crossref","first-page":"6177","DOI":"10.1021\/jm051256o","article-title":"Extra precision glide: docking and scoring incorporating a model of hydrophobic enclosure for protein-ligand complexes","volume":"49","author":"Friesner","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2022.102454_bib92","doi-asserted-by":"crossref","first-page":"1932","DOI":"10.1021\/ci500118s","article-title":"Docking covalent inhibitors: a parameter free approach to pose prediction and scoring","volume":"54","author":"Zhu","year":"2014","journal-title":"J.\u00a0Chem. Inf. Model."},{"key":"10.1016\/j.jbc.2022.102454_bib93","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1021\/jm050540c","article-title":"Novel procedure for modeling ligand\/receptor induced fit effects","volume":"49","author":"Sherman","year":"2006","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2022.102454_bib94","series-title":"Schr\u00f6dinger Release 2020-4: Glide","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib95","series-title":"Schr\u00f6dinger Release 2020-4","year":"2020"},{"key":"10.1016\/j.jbc.2022.102454_bib96","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1002\/pro.3280","article-title":"Improvements to the APBS biomolecular solvation software suite","volume":"27","author":"Jurrus","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2022.102454_bib97","doi-asserted-by":"crossref","first-page":"W363","DOI":"10.1093\/nar\/gky473","article-title":"CASTp 3.0: computed atlas of surface topography of proteins","volume":"46","author":"Tian","year":"2018","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jbc.2022.102454_bib98","doi-asserted-by":"crossref","first-page":"W636","DOI":"10.1093\/nar\/gkz268","article-title":"The EMBL-EBI search and sequence analysis tools APIs in 2019","volume":"47","author":"Madeira","year":"2019","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jbc.2022.102454_bib99","doi-asserted-by":"crossref","first-page":"i438","DOI":"10.1093\/bioinformatics\/bts417","article-title":"SANS: high-throughput retrieval of protein sequences allowing 50% mismatches","volume":"28","author":"Koskinen","year":"2012","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jbc.2022.102454_bib100","doi-asserted-by":"crossref","first-page":"W24","DOI":"10.1093\/nar\/gkv317","article-title":"SANSparallel: interactive homology search against uniprot","volume":"43","author":"Somervuo","year":"2015","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.jbc.2022.102454_bib101","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1093\/bioinformatics\/btp033","article-title":"Jalview Version 2\u2014a multiple sequence alignment editor and analysis workbench","volume":"25","author":"Waterhouse","year":"2009","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jbc.2022.102454_bib102","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1101\/gr.849004","article-title":"WebLogo: a sequence logo generator","volume":"14","author":"Crooks","year":"2004","journal-title":"Genome Res."},{"key":"10.1016\/j.jbc.2022.102454_bib103","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1002\/prot.340230412","article-title":"Knowledge-based protein secondary structure assignment","volume":"23","author":"Frishman","year":"1995","journal-title":"Proteins"},{"key":"10.1016\/j.jbc.2022.102454_bib104","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.jbc.2022.102454_bib105","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1002\/pro.3330","article-title":"MolProbity: more and better reference data for improved all-atom structure validation","volume":"27","author":"Williams","year":"2018","journal-title":"Protein Sci."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822008973?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822008973?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T20:53:48Z","timestamp":1777409628000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925822008973"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,10]]},"references-count":105,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2022,10]]}},"alternative-id":["S0021925822008973"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102454","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2022.03.18.483834","asserted-by":"object"}]},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2022,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"High-resolution structures of a siderophore-producing cyclization domain from Yersinia pestis offer a refined proposal of substrate binding","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102454","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"102454"}}