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dc.contributor.authorHare, Sen_US
dc.contributor.authorFischer, Wen_US
dc.contributor.authorWilliams, Ren_US
dc.contributor.authorTerradot, Len_US
dc.contributor.authorBayliss, Ren_US
dc.contributor.authorHaas, Ren_US
dc.contributor.authorWaksman, Gen_US
dc.date.accessioned2018-08-30T13:49:11Z
dc.date.issued2007-11en_US
dc.identifier23en_US
dc.identifier.citationEMBO JOURNAL, 2007, 26 pp. 4926 - 4934en_US
dc.identifier.issn0261-4189en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/2463
dc.identifier.eissn1460-2075en_US
dc.identifier.doi10.1038/sj.emboj.7601904en_US
dc.description.abstractHelicobacter pylori is one of the world’s most successful human pathogens causing gastric ulcers and cancers. A key virulence factor of H. pylori is the Cag pathogenicity island, which encodes a type IV secretion system. HP0525 is an essential component of the Cag system and acts as an inner membrane associated ATPase. HP0525 forms double hexameric ring structures, with the C-terminal domains (CTDs) forming a closed ring and the N- terminal domains (NTDs) forming a dynamic, open ring. Here, the crystal structure of HP0525 in complex with a fragment of HP1451, a protein of previously unknown function, is reported. The HP1451 construct consists of two domains similar to nucleic acid- binding domains. Two HP1451 molecules bind to the HP0525 NTDs on opposite sides of the hexamer, locking it in the closed form and forming a partial lid over the HP0525 chamber. From the structure, it is suggested that HP1451 acts as an inhibitory factor of HP0525 to regulate Cag- mediated secretion, a suggestion confirmed by results of in vitro ATPase assay and in vivo pull-down experiments.en_US
dc.format.extent4926 - 4934en_US
dc.languageEnglishen_US
dc.language.isoEnglishen_US
dc.publisherWILEY-BLACKWELLen_US
dc.titleIdentification, structure and mode of action of a new regulator of the Helicobacter pylori HP0525 ATPaseen_US
dc.typeJournal Article
rioxxterms.versionofrecord10.1038/sj.emboj.7601904en_US
rioxxterms.licenseref.startdate2007-11en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfEMBO JOURNALen_US
pubs.notesaffiliation: Waksman, G (Reprint Author), Univ London Birkbeck Coll, Sch Crystallograph, Inst Struct Mol Biol, Malet Str, London WC1E 7HX, England. Birkbeck Coll, Sch Crystallograph, London, England. UCL, Inst Struct Mol Biol, London, England. Max Von Pettenkofer Inst Hyg & Med Microbiol, Munich, Germany. Imperial Coll London, Fac Med, Dept Infect Dis, London W2 1PG, England. ESRF, CIBB, Macromol Crystallograph Grp, Grenoble, France. Inst Canc Res, Sect Struct Biol, London SW3 6JB, England. keywords: ATPase; crystal structure; Helicobacter pylori; type IV secretion; VirB11 keywords-plus: IV SECRETION SYSTEMS; GASTRIC EPITHELIAL-CELLS; PROTEIN-INTERACTION MAP; CAGA PROTEIN; LEGIONELLA-PNEUMOPHILA; BACTERIAL CONJUGATION; BORDETELLA-PERTUSSIS; BRUCELLA-SUIS; KH DOMAIN; TRANSLOCATION research-areas: Biochemistry & Molecular Biology; Cell Biology web-of-science-categories: Biochemistry & Molecular Biology; Cell Biology author-email: [email protected] orcid-numbers: Hare, Stephen/0000-0003-2951-1595 Bayliss, Richard/0000-0003-0604-2773 funding-acknowledgement: Wellcome Trust [065932] number-of-cited-references: 41 times-cited: 22 usage-count-last-180-days: 0 usage-count-since-2013: 3 journal-iso: Embo J. doc-delivery-number: 236DE unique-id: ISI:000251282400012 oa: gold_or_bronze da: 2018-08-30en_US
pubs.notesNot knownen_US
pubs.organisational-group/ICR
pubs.volume26en_US
pubs.embargo.termsNot knownen_US
dc.contributor.icrauthorBayliss, Richarden_US


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