{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T02:25:47Z","timestamp":1784600747449,"version":"3.55.0"},"reference-count":68,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2023,1,1]],"date-time":"2023-01-01T00:00:00Z","timestamp":1672531200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,1,1]],"date-time":"2023-01-01T00:00:00Z","timestamp":1672531200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,11,30]],"date-time":"2022-11-30T00:00:00Z","timestamp":1669766400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2023,1]]},"DOI":"10.1016\/j.jbc.2022.102762","type":"journal-article","created":{"date-parts":[[2022,12,1]],"date-time":"2022-12-01T14:10:39Z","timestamp":1669903839000},"page":"102762","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["The structure of caseinolytic protease subunit ClpP2 reveals a functional model of the caseinolytic protease system from Chlamydia trachomatis"],"prefix":"10.1016","volume":"299","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3615-7785","authenticated-orcid":false,"given":"Jahaun","family":"Azadmanesh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed A.","family":"Seleem","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucas","family":"Struble","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2527-5441","authenticated-orcid":false,"given":"Nicholas A.","family":"Wood","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Derek J.","family":"Fisher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4217-8371","authenticated-orcid":false,"given":"Jeffrey J.","family":"Lovelace","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio","family":"Artigues","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aron W.","family":"Fenton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gloria E.O.","family":"Borgstahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3721-6839","authenticated-orcid":false,"given":"Scot P.","family":"Ouellette","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3568-2545","authenticated-orcid":false,"given":"Martin","family":"Conda-Sheridan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2022.102762_bib1","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1093\/humupd\/5.5.433","article-title":"Chlamydia trachomatis: impact on human reproduction","volume":"5","author":"Paavonen","year":"1999","journal-title":"Hum. Reprod. Update"},{"key":"10.1016\/j.jbc.2022.102762_bib2","series-title":"New CDC Analysis Shows Steep and Sustained Increases in STDs in Recent Years","author":"Control","year":"2017"},{"key":"10.1016\/j.jbc.2022.102762_bib3","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.2217\/fmb.10.96","article-title":"Antibiotic resistance in chlamydiae","volume":"5","author":"Sandoz","year":"2010","journal-title":"Future Microbiol."},{"key":"10.1016\/j.jbc.2022.102762_bib4","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1038\/s41598-018-36601-y","article-title":"Autophagy induction and PDGFR-\u03b2 knockdown by siRNA-encapsulated nanoparticles reduce chlamydia trachomatis infection","volume":"9","author":"Yang","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102762_bib5","doi-asserted-by":"crossref","first-page":"9393","DOI":"10.1021\/acs.jmedchem.7b00716","article-title":"Thiazolino 2-pyridone amide isosteres as inhibitors of Chlamydia trachomatis infectivity","volume":"60","author":"Good","year":"2017","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib6","doi-asserted-by":"crossref","first-page":"3269","DOI":"10.3389\/fmicb.2018.03269","article-title":"A\u00a0synthetic, small, sulfated agent is a promising inhibitor of Chlamydia spp. infection in\u00a0vivo","volume":"9","author":"Gallegos","year":"2019","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2022.102762_bib7","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.femsre.2005.03.002","article-title":"The chlamydial developmental cycle","volume":"29","author":"Abdelrahman","year":"2005","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.jbc.2022.102762_bib8","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0149011","article-title":"Quantitative proteomics of the infectious and replicative forms of Chlamydia trachomatis","volume":"11","author":"Skipp","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2022.102762_bib9","doi-asserted-by":"crossref","first-page":"3540","DOI":"10.1074\/mcp.M116.061986","article-title":"Quantitative protein profiling of Chlamydia trachomatis growth forms reveals defense strategies against tryptophan starvation","volume":"15","author":"Ostergaard","year":"2016","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.jbc.2022.102762_bib10","first-page":"592","article-title":"Regulation by proteolysis: energy-dependent proteases and their targets","volume":"56","author":"Gottesman","year":"1992","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.jbc.2022.102762_bib11","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/j.chembiol.2011.07.023","article-title":"Activators of cylindrical proteases as antimicrobials: identification and development of small molecule activators of ClpP protease","volume":"18","author":"Leung","year":"2011","journal-title":"Chem. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib12","doi-asserted-by":"crossref","first-page":"17474","DOI":"10.1073\/pnas.1110385108","article-title":"Antibiotic acyldepsipeptides activate ClpP peptidase to degrade the cell division protein FtsZ","volume":"108","author":"Sass","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102762_bib13","doi-asserted-by":"crossref","first-page":"e00253-15","DOI":"10.1128\/mBio.00253-15","article-title":"Target mechanism-based whole-cell screening identifies bortezomib as an inhibitor of caseinolytic protease in mycobacteria","volume":"6","author":"Moreira","year":"2015","journal-title":"mBio"},{"key":"10.1016\/j.jbc.2022.102762_bib14","doi-asserted-by":"crossref","first-page":"5662","DOI":"10.1016\/j.bmc.2017.08.049","article-title":"A\u00a0novel class of Plasmodial ClpP protease inhibitors as potential antimalarial agents","volume":"25","author":"Mundra","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib15","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/nature12790","article-title":"Activated ClpP kills persisters and eradicates a chronic biofilm infection","volume":"503","author":"Conlon","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102762_bib16","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1021\/acsinfecdis.1c00553","article-title":"In\u00a0vitro and in\u00a0vivo activity of (Trifluoromethyl)pyridines as anti-Chlamydia trachomatis agents","volume":"8","author":"Seleem","year":"2022","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.jbc.2022.102762_bib17","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.02016-20","article-title":"The ClpX and ClpP2 orthologs of Chlamydia trachomatis perform discrete and essential functions in organism growth and development","volume":"11","author":"Wood","year":"2020","journal-title":"mBio"},{"key":"10.1016\/j.jbc.2022.102762_bib18","article-title":"Initial characterization of the two ClpP paralogs of Chlamydia trachomatis suggests unique functionality for each","volume":"201","author":"Wood","year":"2019","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2022.102762_bib19","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/S1097-2765(03)00060-1","article-title":"Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals","volume":"11","author":"Flynn","year":"2003","journal-title":"Mol. Cel."},{"key":"10.1016\/j.jbc.2022.102762_bib20","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.ymben.2015.06.005","article-title":"An ensemble-guided approach identifies ClpP as a major regulator of transcript levels in nitric oxide-stressed Escherichia coli","volume":"31","author":"Robinson","year":"2015","journal-title":"Metab. Eng."},{"key":"10.1016\/j.jbc.2022.102762_bib21","doi-asserted-by":"crossref","first-page":"18201","DOI":"10.1016\/S0021-9258(17)32435-3","article-title":"Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates","volume":"269","author":"Thompson","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib22","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002511","article-title":"Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in\u00a0vitro and during infection","volume":"8","author":"Raju","year":"2012","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2022.102762_bib23","doi-asserted-by":"crossref","first-page":"14394","DOI":"10.1074\/jbc.M700275200","article-title":"Distinctive types of ATP-dependent Clp proteases in cyanobacteria","volume":"282","author":"Stanne","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib24","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1126\/science.282.5389.754","article-title":"Genome sequence of an obligate intracellular pathogen of humans: chlamydia trachomatis","volume":"282","author":"Stephens","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.jbc.2022.102762_bib25","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1128\/JB.06142-11","article-title":"Validation of the essential ClpP protease in Mycobacterium tuberculosis as a novel drug target","volume":"194","author":"Ollinger","year":"2012","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2022.102762_bib26","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1038\/emboj.2012.5","article-title":"The active ClpP protease from M.\u00a0tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring","volume":"31","author":"Akopian","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2022.102762_bib27","doi-asserted-by":"crossref","first-page":"3598","DOI":"10.1002\/anie.201409325","article-title":"Structure and mechanism of the caseinolytic protease ClpP1\/2 heterocomplex from Listeria monocytogenes","volume":"54","author":"Dahmen","year":"2015","journal-title":"Angew. Chem. Int. Edition"},{"key":"10.1016\/j.jbc.2022.102762_bib28","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1039\/C6SC03438A","article-title":"Insights into ClpXP proteolysis: heterooligomerization and partial deactivation enhance chaperone affinity and substrate turnover in Listeria monocytogenes","volume":"8","author":"Balogh","year":"2017","journal-title":"Chem. Sci."},{"key":"10.1016\/j.jbc.2022.102762_bib29","doi-asserted-by":"crossref","first-page":"e00568-16","DOI":"10.1128\/JB.00568-16","article-title":"Two isoforms of Clp peptidase in Pseudomonas aeruginosa control distinct aspects of cellular physiology","volume":"199","author":"Hall","year":"2017","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.jbc.2022.102762_bib30","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-50505-5","article-title":"The functional ClpXP protease of Chlamydia trachomatis requires distinct clpP genes from separate genetic loci","volume":"9","author":"Pan","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jbc.2022.102762_bib31","doi-asserted-by":"crossref","first-page":"4508","DOI":"10.1016\/j.jmb.2013.08.005","article-title":"Activation of ClpP protease by ADEP antibiotics: Insights from hydrogen exchange mass spectrometry","volume":"425","author":"Sowole","year":"2013","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib32","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1038\/s41594-019-0304-0","article-title":"Cryo-EM structure of the ClpXP protein degradation machinery","volume":"26","author":"Gatsogiannis","year":"2019","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib33","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.52774","article-title":"Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate","volume":"9","author":"Fei","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2022.102762_bib34","doi-asserted-by":"crossref","first-page":"eaaw3818","DOI":"10.1126\/sciadv.aaw3818","article-title":"Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors","volume":"5","author":"Felix","year":"2019","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2022.102762_bib35","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1111\/mmi.12356","article-title":"Structural determinants stabilizing the axial channel of ClpP for substrate translocation","volume":"90","author":"Alexopoulos","year":"2013","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2022.102762_bib36","doi-asserted-by":"crossref","first-page":"400","DOI":"10.3109\/10409238.2014.925421","article-title":"Dynamics of the ClpP serine protease: a model for self-compartmentalized proteases","volume":"49","author":"Liu","year":"2014","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib37","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1038\/nm1306","article-title":"Dysregulation of bacterial proteolytic machinery by a new class of antibiotics","volume":"11","author":"Brotz-Oesterhelt","year":"2005","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2022.102762_bib38","doi-asserted-by":"crossref","first-page":"5895","DOI":"10.1073\/pnas.1921630117","article-title":"An allosteric switch regulates Mycobacterium tuberculosis ClpP1P2 protease function as established by cryo-EM and methyl-TROSY NMR","volume":"117","author":"Vahidi","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102762_bib39","doi-asserted-by":"crossref","first-page":"11302","DOI":"10.1073\/pnas.1219125110","article-title":"Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad","volume":"110","author":"Zeiler","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2022.102762_bib40","doi-asserted-by":"crossref","first-page":"5749","DOI":"10.1002\/anie.201100666","article-title":"A\u00a0conformational switch underlies ClpP protease function","volume":"50","author":"Geiger","year":"2011","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jbc.2022.102762_bib41","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1016\/j.str.2010.04.008","article-title":"Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations","volume":"18","author":"Kimber","year":"2010","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2022.102762_bib42","doi-asserted-by":"crossref","first-page":"3749","DOI":"10.1016\/j.febslet.2007.04.076","article-title":"ClpP: a distinctive family of cylindrical energy-dependent serine proteases","volume":"581","author":"Yu","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2022.102762_bib43","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.1111\/mmi.14649","article-title":"ClpP1P2 peptidase activity promotes biofilm formation in Pseudomonas aeruginosa","volume":"115","author":"Mawla","year":"2021","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2022.102762_bib44","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/84967","article-title":"Molecular determinants of complex formation between Clp\/Hsp100 ATPases and the ClpP peptidase","volume":"8","author":"Kim","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib45","doi-asserted-by":"crossref","first-page":"17643","DOI":"10.1074\/jbc.M113.452714","article-title":"Helix unfolding\/refolding characterizes the functional dynamics of Staphylococcus aureus Clp protease","volume":"288","author":"Ye","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib46","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1038\/s42003-019-0656-3","article-title":"ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores","volume":"2","author":"Mabanglo","year":"2019","journal-title":"Commun. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib47","doi-asserted-by":"crossref","first-page":"3224","DOI":"10.1021\/acsinfecdis.0c00599","article-title":"Development of antibiotics that dysregulate the neisserial ClpP protease","volume":"6","author":"Binepal","year":"2020","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.jbc.2022.102762_bib48","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2022.102762_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.jbc.2022.101781","article-title":"Recent structural insights into the mechanism of ClpP protease regulation by AAA+ chaperones and small molecules","volume":"298","author":"Mabanglo","year":"2022","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib50","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1039\/C6MB00644B","article-title":"The development of small-molecule modulators for ClpP protease activity","volume":"13","author":"Ye","year":"2016","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.jbc.2022.102762_bib51","doi-asserted-by":"crossref","first-page":"7465","DOI":"10.1074\/jbc.M115.700344","article-title":"Structure and functional properties of the active form of the proteolytic complex, ClpP1P2, from Mycobacterium tuberculosis","volume":"291","author":"Li","year":"2016","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib52","doi-asserted-by":"crossref","first-page":"2232","DOI":"10.3390\/ijms20092232","article-title":"ClpP protease, a promising antimicrobial target","volume":"20","author":"Moreno-Cinos","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.jbc.2022.102762_bib53","doi-asserted-by":"crossref","first-page":"4370","DOI":"10.1021\/acs.jmedchem.0c00371","article-title":"Synthesis and antichlamydial activity of molecules based on dysregulators of cylindrical proteases","volume":"63","author":"Seleem","year":"2020","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.jbc.2022.102762_bib54","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S0304-3991(03)00053-6","article-title":"Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials","volume":"97","author":"Shlyakhtenko","year":"2003","journal-title":"Ultramicroscopy"},{"key":"10.1016\/j.jbc.2022.102762_bib55","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1007\/978-1-62703-776-1_17","article-title":"Visualization of DNA and protein-DNA complexes with atomic force microscopy","volume":"1117","author":"Lyubchenko","year":"2014","journal-title":"Methods Mol Biol"},{"key":"10.1016\/j.jbc.2022.102762_bib56","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1107\/S0907444910048675","article-title":"iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM","volume":"67","author":"Battye","year":"2011","journal-title":"Acta Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib57","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1107\/S0907444905036693","article-title":"Scaling and assessment of data quality","volume":"62","author":"Evans","year":"2006","journal-title":"Acta Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib58","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn","year":"2011","journal-title":"Acta Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib59","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/S0076-6879(97)76068-3","article-title":"Detecting and overcoming crystal twinning","volume":"276","author":"Yeates","year":"1997","journal-title":"Met. Enzymol."},{"key":"10.1016\/j.jbc.2022.102762_bib60","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 Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib61","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.2022.102762_bib62","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 Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib63","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1107\/S1399004714028132","article-title":"Fem: feature-enhanced map","volume":"71","author":"Afonine","year":"2015","journal-title":"Acta Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib64","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ymeth.2011.07.005","article-title":"The Phenix software for automated determination of macromolecular structures","volume":"55","author":"Adams","year":"2011","journal-title":"Methods"},{"key":"10.1016\/j.jbc.2022.102762_bib65","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 Cryst. D"},{"key":"10.1016\/j.jbc.2022.102762_bib66","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1007\/978-3-319-41448-5_19","article-title":"Protein structural analysis via mass spectrometry-based proteomics","volume":"919","author":"Artigues","year":"2016","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.jbc.2022.102762_bib67","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.2022.102762_bib68","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"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822012054?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925822012054?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T00:32:51Z","timestamp":1758241971000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925822012054"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1]]},"references-count":68,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2023,1]]}},"alternative-id":["S0021925822012054"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102762","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2023,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The structure of caseinolytic protease subunit ClpP2 reveals a functional model of the caseinolytic protease system from Chlamydia trachomatis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2022.102762","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":"102762"}}