{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T17:49:14Z","timestamp":1793382554177,"version":"4.5.0"},"reference-count":41,"publisher":"Elsevier BV","issue":"29","license":[{"start":{"date-parts":[[2018,7,1]],"date-time":"2018-07-01T00:00:00Z","timestamp":1530403200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,8,26]],"date-time":"2020-08-26T00:00:00Z","timestamp":1598400000000},"content-version":"vor","delay-in-days":787,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det (VR)","doi-asserted-by":"publisher","award":["2013\u201305930"],"award-info":[{"award-number":["2013\u201305930"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det (VR)","doi-asserted-by":"publisher","award":["2017\u201303827"],"award-info":[{"award-number":["2017\u201303827"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004063","name":"Knut och Alice Wallenbergs Stiftelse (Knut and Alice Wallenberg Foundation)","doi-asserted-by":"publisher","award":["RiboCORE"],"award-info":[{"award-number":["RiboCORE"]}],"id":[{"id":"10.13039\/501100004063","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":[[2018,7]]},"DOI":"10.1074\/jbc.ra118.003989","type":"journal-article","created":{"date-parts":[[2018,6,5]],"date-time":"2018-06-05T11:29:51Z","timestamp":1528198191000},"page":"11481-11490","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":49,"title":["Structural mechanism of AadA, a dual-specificity aminoglycoside adenylyltransferase from Salmonella enterica"],"prefix":"10.1016","volume":"293","author":[{"given":"Ana Laura","family":"Stern","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8783-1194","authenticated-orcid":false,"given":"Sander Egbert","family":"Van der Verren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandesh","family":"Kanchugal P","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joakim","family":"N\u00e4svall","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hugo","family":"Guti\u00e9rrez-de-Ter\u00e1n","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria","family":"Selmer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA118.003989_bib1","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1128\/CMR.16.3.430-450.2003","article-title":"Versatility of aminoglycosides and prospects for their future","volume":"16","author":"Vakulenko","year":"2003","journal-title":"Clin. Microbiol. Rev"},{"key":"10.1074\/jbc.RA118.003989_bib2","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1038\/nrmicro3155","article-title":"Ribosome-targeting antibiotics and mechanisms of bacterial resistance","volume":"12","author":"Wilson","year":"2014","journal-title":"Nat. Rev. Microbiol"},{"key":"10.1074\/jbc.RA118.003989_bib3","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1021\/cb3005116","article-title":"Aminoglycoside antibiotics in the 21st century","volume":"8","author":"Becker","year":"2013","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.RA118.003989_bib4","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1038\/35030019","article-title":"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics","volume":"407","author":"Carter","year":"2000","journal-title":"Nature"},{"key":"10.1074\/jbc.RA118.003989_bib5","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1021\/cb700100n","article-title":"A steric block in translation caused by the antibiotic spectinomycin","volume":"2","author":"Borovinskaya","year":"2007","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.RA118.003989_bib6","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.ijantimicag.2008.09.001","article-title":"Do we still need the aminoglycosides?","volume":"33","author":"Durante-Mangoni","year":"2009","journal-title":"Int. J. Antimicrob. Agents"},{"key":"10.1074\/jbc.RA118.003989_bib7","first-page":"2129","article-title":"Dihydrostreptomycine tegenaangewezen bij \u201clange\u201d kuren. (Dihydrostreptomycin contraindicated in long courses of treatment.)","volume":"94","author":"Minkenhof","year":"1950","journal-title":"Ned. Tijdschr. Geneeeskd"},{"key":"10.1074\/jbc.RA118.003989_bib8","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/S0966-842X(97)01033-0","article-title":"Bacterial resistance to aminoglycoside antibiotics","volume":"5","author":"Davies","year":"1997","journal-title":"Trends Microbiol"},{"key":"10.1074\/jbc.RA118.003989_bib9","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.drup.2010.08.003","article-title":"Aminoglycoside modifying enzymes","volume":"13","author":"Ramirez","year":"2010","journal-title":"Drug Resist. Updat"},{"key":"10.1074\/jbc.RA118.003989_bib10","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1054\/drup.2001.0197","article-title":"Aminoglycoside-modifying enzymes: mechanisms of catalytic processes and inhibition","volume":"4","author":"Azucena","year":"2001","journal-title":"Drug Resist. Updat"},{"key":"10.1074\/jbc.RA118.003989_bib11","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/0147-619X(85)90052-6","article-title":"Nucleotide sequence analysis of a gene encoding a streptomycin\/spectinomycin adenylyltransferase","volume":"13","author":"Hollingshead","year":"1985","journal-title":"Plasmid"},{"key":"10.1074\/jbc.RA118.003989_bib12","doi-asserted-by":"crossref","first-page":"2267","DOI":"10.1107\/S1399004715016429","article-title":"Structure of AadA from Salmonella enterica: a monomeric aminoglycoside (3\u2033)(9) adenyltransferase","volume":"71","author":"Chen","year":"2015","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA118.003989_bib13","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.molcel.2006.03.013","article-title":"Making and breaking nucleic acids: two-Mg2+-ion catalysis and substrate specificity","volume":"22","author":"Yang","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA118.003989_bib14","doi-asserted-by":"crossref","first-page":"13305","DOI":"10.1021\/bi00041a005","article-title":"Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase","volume":"34","author":"Pedersen","year":"1995","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.003989_bib15","doi-asserted-by":"crossref","first-page":"W537","DOI":"10.1093\/nar\/gks375","article-title":"H++ 3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations","volume":"40","author":"Anandakrishnan","year":"2012","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA118.003989_bib16","doi-asserted-by":"crossref","first-page":"1649","DOI":"10.1016\/j.str.2009.10.013","article-title":"Structure and mechanism of the lincosamide antibiotic adenylyltransferase LinB","volume":"17","author":"Morar","year":"2009","journal-title":"Structure"},{"key":"10.1074\/jbc.RA118.003989_bib17","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1021\/acschembio.5b01070","article-title":"Structural analysis of the tobramycin and gentamicin clinical resistome reveals limitations for next-generation aminoglycoside design","volume":"11","author":"Bassenden","year":"2016","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/jbc.RA118.003989_bib18","doi-asserted-by":"crossref","first-page":"D222","DOI":"10.1093\/nar\/gkt1223","article-title":"Pfam: the protein families database","volume":"42","author":"Finn","year":"2014","journal-title":"Nucleic Acids Res"},{"key":"10.1074\/jbc.RA118.003989_bib19","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1128\/AAC.43.1.157","article-title":"Detection of a streptomycin\/spectinomycin adenylyltransferase gene (aadA) in Enterococcus faecalis","volume":"43","author":"Clark","year":"1999","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA118.003989_bib20","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1128\/MR.57.1.138-163.1993","article-title":"Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes","volume":"57","author":"Shaw","year":"1993","journal-title":"Microbiol. Rev"},{"key":"10.1074\/jbc.RA118.003989_bib21","first-page":"152","article-title":"Biophysical and enzymatic properties of aminoglycoside adenylyltransferase AadA6 from Pseudomonas aeruginosa","volume":"4","author":"Papadovasilaki","year":"2015","journal-title":"Biochem. Biophys. Rep"},{"key":"10.1074\/jbc.RA118.003989_bib22","doi-asserted-by":"crossref","first-page":"8368","DOI":"10.1021\/bi060723g","article-title":"Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3\u2033)-Ii\/AAC(6\u2032)-IId from Serratia marcescens","volume":"45","author":"Kim","year":"2006","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA118.003989_bib23","doi-asserted-by":"crossref","first-page":"2454","DOI":"10.1128\/AAC.49.6.2454-2459.2005","article-title":"Mosaic structure of a multiple-drug-resistant, conjugative plasmid from Campylobacter jejuni","volume":"49","author":"Nirdnoy","year":"2005","journal-title":"Antimicrob. Agents Chemother"},{"key":"10.1074\/jbc.RA118.003989_bib24","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. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA118.003989_bib25","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA118.003989_bib26","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA118.003989_bib27","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. Appl. Crystallogr"},{"key":"10.1074\/jbc.RA118.003989_bib28","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":"10.1074\/jbc.RA118.003989_bib29","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":"10.1074\/jbc.RA118.003989_bib30","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for finding protein models in electron density maps and the location of error in these models","volume":"47","author":"Jones","year":"1991","journal-title":"Acta Crystallogr. A"},{"key":"10.1074\/jbc.RA118.003989_bib31","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S1093-3263(02)00140-7","article-title":"Improvements in the analysis of domain motions in proteins from conformational change: DynDom version 1.50","volume":"21","author":"Hayward","year":"2002","journal-title":"J. Mol. Graph. Model"},{"key":"10.1074\/jbc.RA118.003989_bib32","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0022-2836(71)90324-X","article-title":"The interpretation of protein structures: estimation of static accessibility","volume":"55","author":"Lee","year":"1971","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA118.003989_bib33","doi-asserted-by":"crossref","first-page":"e0184126","DOI":"10.1371\/journal.pone.0184126","article-title":"Direct and inverted repeat stimulated excision (DIRex): simple, single-step, and scar-free mutagenesis of bacterial genes","volume":"12","author":"N\u00e4svall","year":"2017","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA118.003989_bib34","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1111\/j.1365-2958.2011.07657.x","article-title":"Activation of cryptic aminoglycoside resistance in Salmonella enterica","volume":"80","author":"Koskiniemi","year":"2011","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA118.003989_bib35","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1038\/nprot.2007.321","article-title":"The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability","volume":"2","author":"Niesen","year":"2007","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.RA118.003989_bib36","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD","volume":"26","author":"Phillips","year":"2005","journal-title":"J. Comput. Chem"},{"key":"10.1074\/jbc.RA118.003989_bib37","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J. Chem. Phys"},{"key":"10.1074\/jbc.RA118.003989_bib38","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph"},{"key":"10.1074\/jbc.RA118.003989_bib39","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":"10.1074\/jbc.RA118.003989_bib40","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1093\/bioinformatics\/btg430","article-title":"The Jalview Java alignment editor","volume":"20","author":"Clamp","year":"2004","journal-title":"Bioinformatics"},{"key":"10.1074\/jbc.RA118.003989_bib41","doi-asserted-by":"crossref","first-page":"3320","DOI":"10.1093\/nar\/gkg556","article-title":"ESPript\/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins","volume":"31","author":"Gouet","year":"2003","journal-title":"Nucleic Acids Res"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820315702?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820315702?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA118.003989","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,3,29]],"date-time":"2021-03-29T13:34:13Z","timestamp":1617024853000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820315702"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,7]]},"references-count":41,"journal-issue":{"issue":"29","published-print":{"date-parts":[[2018,7]]}},"alternative-id":["S0021925820315702"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra118.003989","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural mechanism of AadA, a dual-specificity aminoglycoside adenylyltransferase from Salmonella enterica","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA118.003989","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Stern et al.","name":"copyright","label":"Copyright"}]}}