{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,24]],"date-time":"2026-02-24T09:19:52Z","timestamp":1771924792906,"version":"3.50.1"},"reference-count":51,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2002,10,1]],"date-time":"2002-10-01T00:00:00Z","timestamp":1033430400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":3942,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Structure"],"published-print":{"date-parts":[[2002,10]]},"DOI":"10.1016\/s0969-2126(02)00855-9","type":"journal-article","created":{"date-parts":[[2003,1,21]],"date-time":"2003-01-21T19:54:09Z","timestamp":1043178849000},"page":"1415-1424","source":"Crossref","is-referenced-by-count":97,"title":["Hexameric Ring Structure of the ATPase Domain of the Membrane-Integrated Metalloprotease FtsH from Thermus thermophilus HB8"],"prefix":"10.1016","volume":"10","author":[{"given":"Hajime","family":"Niwa","sequence":"first","affiliation":[]},{"given":"Daisuke","family":"Tsuchiya","sequence":"additional","affiliation":[]},{"given":"Hisayoshi","family":"Makyio","sequence":"additional","affiliation":[]},{"given":"Masasuke","family":"Yoshida","sequence":"additional","affiliation":[]},{"given":"Kosuke","family":"Morikawa","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0969-2126(02)00855-9_BIB1","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1146\/annurev.genet.30.1.465","article-title":"Proteases and their targets in Escherichia coli","volume":"30","author":"Gottesman","year":"1996","journal-title":"Annu. Rev. Genet."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB2","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1128\/jb.175.5.1344-1351.1993","article-title":"The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression","volume":"175","author":"Tomoyasu","year":"1993","journal-title":"J. Bacteriol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB3","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1006\/abbi.2000.1903","article-title":"Escherichia coli requires the protease activity of FtsH for growth","volume":"380","author":"Jayasekera","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB4","doi-asserted-by":"crossref","first-page":"1303","DOI":"10.1046\/j.1365-2958.1997.4231796.x","article-title":"Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli","volume":"24","author":"Shotland","year":"1997","journal-title":"Mol. Microbiol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB5","doi-asserted-by":"crossref","first-page":"3516","DOI":"10.1073\/pnas.92.8.3516","article-title":"Degradation of \u03c3 32, the heat shock regulator in Escherichia coli, is governed by HflB","volume":"92","author":"Herman","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB6","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S0014-5793(00)01869-X","article-title":"Evidence for an active role of the DnaK chaperone system in the degradation of \u03c332","volume":"478","author":"Tatsuta","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB7","doi-asserted-by":"crossref","first-page":"31196","DOI":"10.1074\/jbc.271.49.31196","article-title":"FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins","volume":"271","author":"Akiyama","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB8","doi-asserted-by":"crossref","first-page":"4532","DOI":"10.1073\/pnas.92.10.4532","article-title":"FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit","volume":"92","author":"Kihara","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB9","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/S0014-5793(96)01283-5","article-title":"Subunit a of proton ATPase Fo sector is a substrate of the FtsH protease in Escherichia coli","volume":"399","author":"Akiyama","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB10","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1006\/jmbi.1998.1781","article-title":"Different pathways for protein degradation by the FtsH\/HflKC membrane-embedded protease complex","volume":"279","author":"Kihara","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB11","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.1093\/emboj\/18.11.2970","article-title":"Dislocation of membrane proteins in FtsH-mediated proteolysis","volume":"18","author":"Kihara","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB12","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1038\/18704","article-title":"Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease","volume":"398","author":"Leonhard","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB13","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1128\/jb.175.5.1352-1357.1993","article-title":"Topology and subcellular localization of FtsH protein in Escherichia coli","volume":"175","author":"Tomoyasu","year":"1993","journal-title":"J. Bacteriol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB14","doi-asserted-by":"crossref","first-page":"2043","DOI":"10.1002\/pro.5560061001","article-title":"Sequence analysis of the AAA protein family","volume":"6","author":"Beyer","year":"1997","journal-title":"Protein Sci."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB15","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1101\/gr.9.1.27","article-title":"Aaa+","volume":"9","author":"Neuwald","year":"1999","journal-title":"Genome Res."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB16","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1046\/j.1365-2443.2001.00447.x","article-title":"AAA+ superfamily ATPases","volume":"6","author":"Ogura","year":"2001","journal-title":"Genes Cells"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB17","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0962-8924(97)01212-9","article-title":"The AAA team","volume":"8","author":"Patel","year":"1998","journal-title":"Trends Cell Biol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB18","doi-asserted-by":"crossref","first-page":"2551","DOI":"10.1002\/j.1460-2075.1995.tb07253.x","article-title":"Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor \u03c3 32","volume":"14","author":"Tomoyasu","year":"1995","journal-title":"EMBO J."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB19","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1093\/oxfordjournals.jbchem.a022689","article-title":"FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues","volume":"127","author":"Asahara","year":"2000","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB20","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1016\/S1097-2765(00)00143-X","article-title":"Structure of the AAA ATPase p97","volume":"6","author":"Zhang","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB21","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1006\/jmbi.1993.1489","article-title":"Protein structure comparison by alignment of distance matrices","volume":"233","author":"Holm","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB22","doi-asserted-by":"crossref","first-page":"1442","DOI":"10.1073\/pnas.98.4.1442","article-title":"Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8","volume":"98","author":"Yamada","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB23","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1038\/35001629","article-title":"The structures of HsIU and the ATP-dependent protease HsIU-HsIV","volume":"403","author":"Bochtler","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB24","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/S0092-8674(00)81593-7","article-title":"Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein","volume":"94","author":"Lenzen","year":"1998","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB25","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1016\/S0092-8674(00)00166-5","article-title":"Crystal and solution structures of an HslUV protease-chaperone complex","volume":"103","author":"Sousa","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB26","doi-asserted-by":"crossref","first-page":"23485","DOI":"10.1074\/jbc.270.40.23485","article-title":"FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli","volume":"270","author":"Akiyama","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB27","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0092-8674(00)81648-7","article-title":"Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7","volume":"99","author":"Sawaya","year":"1999","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB28","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/S0092-8674(00)80871-5","article-title":"Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides","volume":"101","author":"Singleton","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB29","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1038\/nsb0997-677","article-title":"Turning off the Ras switch with the flick of a finger","volume":"4","author":"Noel","year":"1997","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB30","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1046\/j.1365-2958.2000.01842.x","article-title":"Mutational analysis of the functional motifs of RuvB, an AAA+ class helicase and motor protein for Holliday junction branch migration","volume":"36","author":"Iwasaki","year":"2000","journal-title":"Mol. Microbiol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB31","doi-asserted-by":"crossref","first-page":"26225","DOI":"10.1074\/jbc.274.37.26225","article-title":"Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH","volume":"274","author":"Karata","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB32","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1046\/j.1365-2958.2001.02301.x","article-title":"Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modeling and mutagenesis","volume":"39","author":"Karata","year":"2001","journal-title":"Mol. Microbiol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB33","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1016\/S0969-2126(01)00670-0","article-title":"Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU","volume":"9","author":"Wang","year":"2001","journal-title":"Structure"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB34","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1046\/j.1365-2958.1998.00843.x","article-title":"Polypeptide binding of Escherichia coli FtsH (HflB)","volume":"28","author":"Akiyama","year":"1998","journal-title":"Mol. Microbiol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB35","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1016\/S1097-2765(00)00144-1","article-title":"A major conformational change in p97 AAA ATPase upon ATP binding","volume":"6","author":"Rouiller","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB36","doi-asserted-by":"crossref","first-page":"6678","DOI":"10.1073\/pnas.96.12.6678","article-title":"Lon and Clp family proteases and chaperones share homologous substrate-recognition domains","volume":"96","author":"Smith","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB37","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1016\/S1097-2765(00)00148-9","article-title":"Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP","volume":"6","author":"Ortega","year":"2000","journal-title":"Mol. Cell"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB38","doi-asserted-by":"crossref","first-page":"3768","DOI":"10.1073\/pnas.071043698","article-title":"ClpA mediates directional translocation of substrate proteins into the ClpP protease","volume":"98","author":"Reid","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB39","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0969-2126(01)00570-6","article-title":"Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism","volume":"9","author":"Wang","year":"2001","journal-title":"Structure"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB40","doi-asserted-by":"crossref","first-page":"14103","DOI":"10.1073\/pnas.250491797","article-title":"Mutational studies on HslU and its docking mode with HslV","volume":"97","author":"Song","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB41","doi-asserted-by":"crossref","first-page":"1888","DOI":"10.1126\/science.286.5446.1888","article-title":"Posttranslational quality control","volume":"286","author":"Wickner","year":"1999","journal-title":"Science"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB42","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1107\/S0907444902006972","article-title":"Crystallization of the AAA domain of the ATP-dependent protease FtsH of Escherichia coli","volume":"58","author":"Krzywda","year":"2002","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB43","series-title":"Crystal Computing","article-title":"Macromolecular data processing","author":"Leslie","year":"1991"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB44","first-page":"760","article-title":"Collaborative Computational Project 4) The CCP4 suite","volume":"50","author":"CCP4","year":"1994","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB45","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collection in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB46","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1107\/S0907444999000839","article-title":"Automated MAD and MIR structure solution","volume":"55","author":"Terwilliger","year":"1999","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB47","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system","volume":"54","author":"Brunger","year":"1998","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB48","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1107\/S0021889891004399","article-title":"Molscript","volume":"24","author":"Kraulis","year":"1991","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB49","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/S0076-6879(97)77028-9","article-title":"Raster3D-photorealistic molecular graphics","volume":"277","author":"Merrit","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0969-2126(02)00855-9_BIB50","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1107\/S0907444998017363","article-title":"Further additions to MolScript version 1.4, including reading and contouring of electron-density maps","volume":"55","author":"Esnouf","year":"1999","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/S0969-2126(02)00855-9_BIB51","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1002\/jcc.540120405","article-title":"A rapid finite-difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation","volume":"12","author":"Nicholls","year":"1991","journal-title":"J. Comput. Chem."}],"container-title":["Structure"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212602008559?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969212602008559?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,25]],"date-time":"2023-04-25T18:30:29Z","timestamp":1682447429000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969212602008559"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2002,10]]},"references-count":51,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2002,10]]}},"alternative-id":["S0969212602008559"],"URL":"https:\/\/doi.org\/10.1016\/s0969-2126(02)00855-9","relation":{},"ISSN":["0969-2126"],"issn-type":[{"value":"0969-2126","type":"print"}],"subject":[],"published":{"date-parts":[[2002,10]]}}}