{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T15:44:43Z","timestamp":1781970283334,"version":"3.54.5"},"reference-count":32,"publisher":"Elsevier BV","issue":"50","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,13]],"date-time":"2021-01-13T00:00:00Z","timestamp":1610496000000},"content-version":"vor","delay-in-days":43,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology, Ministry of Science and Technology, India","doi-asserted-by":"publisher","award":["BT\/03\/IYBA\/2010"],"award-info":[{"award-number":["BT\/03\/IYBA\/2010"]}],"id":[{"id":"10.13039\/501100001407","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":[[2020,12]]},"DOI":"10.1074\/jbc.ra120.014083","type":"journal-article","created":{"date-parts":[[2020,9,30]],"date-time":"2020-09-30T23:45:11Z","timestamp":1601509511000},"page":"16960-16974","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":16,"title":["The heptameric structure of the flagellar regulatory protein FlrC is indispensable for ATPase activity and disassembled by cyclic-di-GMP"],"prefix":"10.1016","volume":"295","author":[{"given":"Shrestha","family":"Chakraborty","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maitree","family":"Biswas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sanjay","family":"Dey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shubhangi","family":"Agarwal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tulika","family":"Chakrabortty","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Biplab","family":"Ghosh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jhimli","family":"Dasgupta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.014083_bib1","doi-asserted-by":"crossref","first-page":"S105","DOI":"10.1093\/infdis\/136.Supplement.S105","article-title":"Mechanisms of disease and immunity in cholera: a review","volume":"136","author":"Holmgren","year":"1977","journal-title":"J. Infect. Dis"},{"key":"10.1074\/jbc.RA120.014083_bib2","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1073\/pnas.84.9.2833","article-title":"Use of phoA gene fusions to identify a pilus colonization factor coordinately regulated with cholera toxin","volume":"84","author":"Taylor","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.014083_bib3","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.tim.2008.12.004","article-title":"Vibrio biofilms: so much the same yet so different","volume":"17","author":"Yildiz","year":"2009","journal-title":"Trends Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib4","doi-asserted-by":"crossref","first-page":"6555","DOI":"10.1128\/JB.00949-09","article-title":"The Vibrio cholerae flagellar regulatory hierarchy controls expression of virulence factors","volume":"191","author":"Syed","year":"2009","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014083_bib5","doi-asserted-by":"crossref","first-page":"1595","DOI":"10.1046\/j.1365-2958.2001.02348.x","article-title":"The novel \u03c354- and \u03c328-dependent flagellar gene transcription hierarchy of Vibrio cholerae","volume":"39","author":"Prouty","year":"2001","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib6","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1046\/j.1365-2958.1998.00809.x","article-title":"Distinct roles of an alternative sigma factor during both free-swimming and colonizing phases of the Vibrio cholerae pathogenic cycle","volume":"28","author":"Klose","year":"1998","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib7","doi-asserted-by":"crossref","first-page":"131","DOI":"10.3389\/fcimb.2019.00131","article-title":"Vibrio flagellar synthesis","volume":"9","author":"Echazarreta","year":"2019","journal-title":"Front. Cell. Infect. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib8","doi-asserted-by":"crossref","first-page":"3158","DOI":"10.1128\/JB.187.9.3158-3170.2005","article-title":"Characterization of enhancer binding by the Vibrio cholerae flagellar regulatory protein FlrC","volume":"187","author":"Correa","year":"2005","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014083_bib9","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.mib.2017.01.002","article-title":"The ins and outs of cyclic di-GMP signaling in Vibrio cholerae","volume":"36","author":"Conner","year":"2017","journal-title":"Curr. Opin. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib10","doi-asserted-by":"crossref","first-page":"3600","DOI":"10.1128\/JB.188.10.3600-3613.2006","article-title":"Transcriptome and phenotypic responses of Vibrio cholerae to increased cyclic di-GMP level","volume":"188","author":"Beyhan","year":"2006","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014083_bib11","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1111\/mmi.12432","article-title":"Cyclic di-GMP inhibits Vibrio cholerae motility by repressing induction of transcription and inducing extracellular polysaccharide production","volume":"90","author":"Srivastava","year":"2013","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib12","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/6d6bf70a-03e1-4612-b75e-b89bd334fbc4","article-title":"Cellular levels and binding of c-di-GMP control subcellular localization and activity of the Vibrio cholerae transcriptional regulator VpsT","volume":"8","author":"Shikuma","year":"2012","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.RA120.014083_bib13","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1046\/j.1365-2958.2000.01745.x","article-title":"Phosphorylation of the flagellar regulatory protein FlrC is necessary for Vibrio cholerae motility and enhanced colonization","volume":"35","author":"Correa","year":"2000","journal-title":"Mol. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib14","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/S1369-5274(00)00179-X","article-title":"Transcriptional regulation at a distance in bacteria","volume":"4","author":"Xu","year":"2001","journal-title":"Curr. Opin. Microbiol"},{"key":"10.1074\/jbc.RA120.014083_bib15","doi-asserted-by":"crossref","first-page":"5251","DOI":"10.1128\/JB.184.19.5251-5260.2002","article-title":"FleQ, the major flagellar gene regulator in Pseudomonas aeruginosa, binds to enhancer sites located either upstream or atypically downstream of the RpoN binding site","volume":"184","author":"Jyot","year":"2002","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014083_bib16","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1128\/MMBR.00006-12","article-title":"The role of bacterial enhancer binding proteins as specialized activators of \u03c354-dependent transcription","volume":"76","author":"Bush","year":"2012","journal-title":"Microbiol. Mol. Biol. Rev"},{"key":"10.1074\/jbc.RA120.014083_bib17","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1016\/j.str.2010.08.018","article-title":"Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase","volume":"18","author":"Chen","year":"2010","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.014083_bib18","doi-asserted-by":"crossref","first-page":"2500","DOI":"10.1101\/gad.229385.113","article-title":"Nucleotide-induced asymmetry within ATPase activator ring drives \u03c354\u2013RNAP interaction and ATP hydrolysis","volume":"27","author":"Sysoeva","year":"2013","journal-title":"Genes Dev"},{"key":"10.1074\/jbc.RA120.014083_bib19","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.molcel.2012.06.012","article-title":"ATPase site architecture is required for self-assembly and remodeling activity of a hexameric AAA+ transcriptional activator","volume":"47","author":"Joly","year":"2012","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.014083_bib20","doi-asserted-by":"crossref","first-page":"8734","DOI":"10.1074\/jbc.M114.611434","article-title":"Unique ATPase site architecture triggers cis-mediated synchronized ATP binding in heptameric AAA+-ATPase domain of flagellar regulatory protein FlrC","volume":"290","author":"Dey","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014083_bib21","doi-asserted-by":"crossref","first-page":"15178","DOI":"10.1074\/jbc.M110.103150","article-title":"Engineered interfaces of an AAA+-ATPase reveal a new nucleotide-dependent coordination mechanism","volume":"285","author":"Joly","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014083_bib22","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.jmb.2005.12.052","article-title":"Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF","volume":"357","author":"Rappas","year":"2006","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.014083_bib23","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1107\/S1744309113015613","article-title":"Purification, crystallization and preliminary X-ray analysis of the AAA+ \u03c354 activator domain of FlrC from Vibrio cholerae","volume":"69","author":"Dey","year":"2013","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun"},{"key":"10.1074\/jbc.RA120.014083_bib24","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/0003-2697(91)90194-X","article-title":"A malachite green colorimetric assay for protein phosphatase activity","volume":"192","author":"Geladopoulos","year":"1991","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA120.014083_bib25","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1128\/JB.01020-07","article-title":"Characterization of nucleotide pools as a function of physiological state in Escherichia coli","volume":"190","author":"Buckstein","year":"2008","journal-title":"J. Bacteriol"},{"key":"10.1074\/jbc.RA120.014083_bib26","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/j.str.2015.04.002","article-title":"Signal transduction in histidine kinases: insights from new structures","volume":"23","author":"Bhate","year":"2015","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.014083_bib27","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1101\/gad.1125603","article-title":"Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains","volume":"17","author":"Lee","year":"2003","journal-title":"Genes Dev"},{"key":"10.1074\/jbc.RA120.014083_bib28","doi-asserted-by":"crossref","first-page":"E209","DOI":"10.1073\/pnas.1523148113","article-title":"Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa","volume":"113","author":"Matsuyama","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.014083_bib29","doi-asserted-by":"crossref","first-page":"24470","DOI":"10.1074\/jbc.M115.661439","article-title":"Bacterial rotary export ATPases are allosterically regulated by the nucleotide second messenger cyclic-di-GMP","volume":"290","author":"Trampari","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.014083_bib30","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":"10.1074\/jbc.RA120.014083_bib31","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":"10.1074\/jbc.RA120.014083_bib32","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1093\/nar\/gkh340","article-title":"MUSCLE: multiple sequence alignment with high accuracy and high throughput","volume":"32","author":"Edgar","year":"2004","journal-title":"Nucleic Acids Res"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192581750592X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192581750592X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.014083","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,31]],"date-time":"2021-12-31T17:20:21Z","timestamp":1640971221000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192581750592X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":32,"journal-issue":{"issue":"50","published-print":{"date-parts":[[2020,12]]}},"alternative-id":["S002192581750592X"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.014083","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The heptameric structure of the flagellar regulatory protein FlrC is indispensable for ATPase activity and disassembled by cyclic-di-GMP","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.014083","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Chakraborty et al.","name":"copyright","label":"Copyright"}]}}