{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T04:13:43Z","timestamp":1792210423728,"version":"4.4.0"},"reference-count":36,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2009,9,1]],"date-time":"2009-09-01T00:00:00Z","timestamp":1251763200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Structural Biology"],"published-print":{"date-parts":[[2009,9]]},"DOI":"10.1016\/j.jsb.2009.06.013","type":"journal-article","created":{"date-parts":[[2009,6,22]],"date-time":"2009-06-22T09:36:51Z","timestamp":1245663411000},"page":"227-234","source":"Crossref","is-referenced-by-count":47,"title":["The AAA+ motor complex of subunits CobS and CobT of cobaltochelatase visualized by single particle electron microscopy"],"prefix":"10.1016","volume":"167","author":[{"given":"Joakim","family":"Lundqvist","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominika","family":"Elmlund","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dana","family":"Heldt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evelyne","family":"Deery","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher A.G.","family":"S\u00f6derberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mats","family":"Hansson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martin","family":"Warren","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Salam","family":"Al-Karadaghi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jsb.2009.06.013_bib1","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.tibs.2006.01.001","article-title":"Chelatases: distort to select?","volume":"31","author":"Al-Karadaghi","year":"2006","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jsb.2009.06.013_bib2","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jsb.2009.06.013_bib3","doi-asserted-by":"crossref","first-page":"3606","DOI":"10.1105\/tpc.106.042374","article-title":"Recessiveness and dominance in barley mutants deficient in Mg-chelatase subunit D, an AAA protein involved in chlorophyll biosynthesis","volume":"18","author":"Axelsson","year":"2006","journal-title":"Plant Cell"},{"key":"10.1016\/j.jsb.2009.06.013_bib4","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1146\/annurev.biochem.72.121801.161828","article-title":"The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes","volume":"72","author":"Banerjee","year":"2003","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jsb.2009.06.013_bib5","doi-asserted-by":"crossref","first-page":"22388","DOI":"10.1074\/jbc.M302468200","article-title":"A story of chelatase evolution: identification and characterization of a small 13\u201315-kDa \u201cancestral\u201d cobaltochelatase (CbiXS) in the archaea","volume":"278","author":"Brindley","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsb.2009.06.013_bib6","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":"10.1016\/j.jsb.2009.06.013_bib7","doi-asserted-by":"crossref","first-page":"892","DOI":"10.1093\/bioinformatics\/14.10.892","article-title":"JPred: a consensus secondary structure prediction server","volume":"14","author":"Cuff","year":"1998","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jsb.2009.06.013_bib8","doi-asserted-by":"crossref","first-page":"7445","DOI":"10.1128\/jb.174.22.7445-7451.1992","article-title":"Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans","volume":"174","author":"Debussche","year":"1992","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jsb.2009.06.013_bib9","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.jsb.2009.04.009","article-title":"High-resolution single-particle orientation refinement based on spectrally self-adapting common lines","volume":"167","author":"Elmlund","year":"2009","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib10","doi-asserted-by":"crossref","first-page":"934","DOI":"10.1016\/j.jmb.2007.11.028","article-title":"A new cryo-EM single-particle ab initio reconstruction method visualizes secondary structure elements in an ATP-fueled AAA+ motor","volume":"375","author":"Elmlund","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib11","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1146\/annurev.biophys.35.040405.101933","article-title":"Evolutionary relationships and structural mechanisms of AAA+ proteins","volume":"35","author":"Erzberger","year":"2006","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.jsb.2009.06.013_bib12","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1006\/jmbi.2001.4834","article-title":"Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase","volume":"311","author":"Fodje","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib13","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/S0076-6879(96)66034-0","article-title":"GOR method for predicting protein secondary structure from amino acid sequence","volume":"266","author":"Garnier","year":"1996","journal-title":"Methods Enzymol."},{"issue":"Pt. 1","key":"10.1016\/j.jsb.2009.06.013_bib14","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1042\/0264-6021:3390127","article-title":"ATPase activity associated with the magnesium-protoporphyrin IX chelatase enzyme of Synechocystis PCC6803: evidence for ATP hydrolysis during Mg2+ insertion, and the MgATP-dependent interaction of the ChlI and ChlD subunits","volume":"339","author":"Jensen","year":"1999","journal-title":"Biochem. J."},{"issue":"Pt. 2","key":"10.1016\/j.jsb.2009.06.013_bib15","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1042\/bj3340335","article-title":"Determinants of catalytic activity with the use of purified I, D and H subunits of the magnesium protoporphyrin IX chelatase from Synechocystis PCC6803","volume":"334","author":"Jensen","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsb.2009.06.013_bib16","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1006\/jmbi.1999.2583","article-title":"GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences","volume":"287","author":"Jones","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib17","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1016\/j.jmb.2008.03.040","article-title":"Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: the role of active site residues","volume":"378","author":"Karlberg","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib18","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/0022-2836(90)90154-E","article-title":"Improvements in protein secondary structure prediction by an enhanced neural network","volume":"214","author":"Kneller","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib19","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","article-title":"Clustal W and Clustal X version 2.0","volume":"23","author":"Larkin","year":"2007","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jsb.2009.06.013_bib20","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0304-3991(00)00106-6","article-title":"Strul \u2013 a method for 3D alignment of single-particle projections based on common line correlation in Fourier space","volume":"87","author":"Lindahl","year":"2001","journal-title":"Ultramicroscopy"},{"key":"10.1016\/j.jsb.2009.06.013_bib21","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1006\/jsbi.1999.4174","article-title":"EMAN: semiautomated software for high-resolution single-particle reconstructions","volume":"128","author":"Ludtke","year":"1999","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib22","doi-asserted-by":"crossref","first-page":"1789","DOI":"10.1073\/pnas.0606144104","article-title":"Substrate interactions with human ferrochelatase","volume":"104","author":"Medlock","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.jsb.2009.06.013_bib23","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1128\/jb.178.3.753-767.1996","article-title":"Salmonella typhimurium cobalamin (vitamin B12) biosynthetic genes: functional studies in S. typhimurium and Escherichia coli","volume":"178","author":"Raux","year":"1996","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jsb.2009.06.013_bib24","doi-asserted-by":"crossref","first-page":"26893","DOI":"10.1074\/jbc.M400958200","article-title":"Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803","volume":"279","author":"Reid","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsb.2009.06.013_bib25","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1042\/bst0300643","article-title":"Current understanding of the function of magnesium chelatase","volume":"30","author":"Reid","year":"2002","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jsb.2009.06.013_bib26","doi-asserted-by":"crossref","first-page":"6912","DOI":"10.1021\/bi034082q","article-title":"The ATPase activity of the ChlI subunit of magnesium chelatase and formation of a heptameric AAA+ ring","volume":"42","author":"Reid","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2009.06.013_bib27","doi-asserted-by":"crossref","first-page":"31294","DOI":"10.1074\/jbc.M805792200","article-title":"Kinetic analyses of the magnesium chelatase provide insights into the mechanism, structure, and formation of the complex","volume":"283","author":"Sawicki","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsb.2009.06.013_bib28","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1042\/bst0300595","article-title":"Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase","volume":"30","author":"Schubert","year":"2002","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.jsb.2009.06.013_bib29","doi-asserted-by":"crossref","first-page":"10660","DOI":"10.1021\/bi9906773","article-title":"Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis","volume":"38","author":"Schubert","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsb.2009.06.013_bib30","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1042\/BJ20061103","article-title":"ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact","volume":"400","author":"Sirijovski","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsb.2009.06.013_bib31","first-page":"19","article-title":"Improved sensitivity of profile searches through the use of sequence weights and gap excision","volume":"10","author":"Thompson","year":"1994","journal-title":"Comput. Appl. Biosci."},{"key":"10.1016\/j.jsb.2009.06.013_bib32","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1042\/bj3270321","article-title":"Mechanism and regulation of Mg-chelatase","volume":"327","author":"Walker","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsb.2009.06.013_bib33","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/0968-0004(90)90304-T","article-title":"Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors","volume":"15","author":"Warren","year":"1990","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.jsb.2009.06.013_bib34","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1039\/b108967f","article-title":"The biosynthesis of adenosylcobalamin (vitamin B12)","volume":"19","author":"Warren","year":"2002","journal-title":"Nat. Prod. Rep."},{"key":"10.1016\/j.jsb.2009.06.013_bib35","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.jsb.2003.11.019","article-title":"EM single particle analysis of the ATP-dependent BchI complex of magnesium chelatase: an AAA+ hexamer","volume":"146","author":"Willows","year":"2004","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jsb.2009.06.013_bib36","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1038\/1843","article-title":"Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP","volume":"5","author":"Yu","year":"1998","journal-title":"Nat. Struct. Biol."}],"container-title":["Journal of Structural Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1047847709001555?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1047847709001555?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,12,18]],"date-time":"2018-12-18T22:22:34Z","timestamp":1545171754000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1047847709001555"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,9]]},"references-count":36,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2009,9]]}},"alternative-id":["S1047847709001555"],"URL":"https:\/\/doi.org\/10.1016\/j.jsb.2009.06.013","relation":{},"ISSN":["1047-8477"],"issn-type":[{"value":"1047-8477","type":"print"}],"subject":[],"published":{"date-parts":[[2009,9]]}}}