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dc.contributor.authorMorales-Ríos, Een
dc.contributor.authorMontgomery, Martinen
dc.contributor.authorLeslie, AGWen
dc.contributor.authorGarcía-Trejo, JJen
dc.contributor.authorWalker, Johnen
dc.date.accessioned2017-08-09T08:44:41Z
dc.date.available2017-08-09T08:44:41Z
dc.date.issued2015-10-01en
dc.identifier.issn2053-230X
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/266071
dc.description.abstractThe structures of F-ATPases have predominantly been determined from mitochondrial enzymes, and those of the enzymes in eubacteria have been less studied. Paracoccus denitrificans is a member of the α-proteobacteria and is related to the extinct protomitochondrion that became engulfed by the ancestor of eukaryotic cells. The P. denitrificans F-ATPase is an example of a eubacterial F-ATPase that can carry out ATP synthesis only, whereas many others can catalyse both the synthesis and the hydrolysis of ATP. Inhibition of the ATP hydrolytic activity of the P. denitrificans F-ATPase involves the ζ inhibitor protein, an α-helical protein that binds to the catalytic F1 domain of the enzyme. This domain is a complex of three α-subunits and three β-subunits, and one copy of each of the γ-, δ- and ℇ-subunits. Attempts to crystallize the F1-ζ inhibitor complex yielded crystals of a subcomplex of the catalytic domain containing the α- and β-subunits only. Its structure was determined to 2.3 Å resolution and consists of a heterodimer of one α-subunit and one β-subunit. It has no bound nucleotides, and it corresponds to the `open' or `empty' catalytic interface found in other F-ATPases. The main significance of this structure is that it aids in the determination of the structure of the intact membrane-bound F-ATPase, which has been crystallized.
dc.description.sponsorshipThis work was funded by the intra-mural program of the Medical Research Council via MRC program U105663150 to J. E. W., and additionally E. M.-R. was supported partially by Consejo Nacional de Ciencia y Tecnología as part of the program ‘Estancias Posdoctorales y Sabáticas en el Extranjero para la Consolidación de Grupos de Investigación’ grant 175676. A. G. W. L. was supported by MRC program U105184325. J.J.G.-T. was supported by grant CB-2011-01-167622 from the Consejo Nacional de Ciencia y Tecnología de México, and grant PAPIIT-IN211012 from the Dirección General de Asuntos del Personal Académico of U.N.A.M.
dc.languageengen
dc.publisherInternational Union of Crystallography
dc.rightsAttribution 4.0 Internationalen
dc.rightsAttribution 4.0 Internationalen
dc.rightsAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectF-ATPaseen
dc.subjectParacoccus denitrificansen
dc.subjectcatalytic αβ dimeren
dc.subjectstructureen
dc.subjectα-proteobacteriaen
dc.subjectBacterial Proteinsen
dc.subjectBiocatalysisen
dc.subjectCrystallizationen
dc.subjectCrystallography, X-Rayen
dc.subjectParacoccus denitrificansen
dc.subjectProtein Multimerizationen
dc.subjectProtein Subunitsen
dc.subjectProton-Translocating ATPasesen
dc.titleStructure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.en
dc.typeArticle
prism.endingPage1317
prism.issueIdentifier10en
prism.publicationDate2015en
prism.publicationNameActa Crystallographica Section F: Structural Biology Communicationsen
prism.startingPage1309
prism.volume71en
dc.identifier.doi10.17863/CAM.9992
dcterms.dateAccepted2015-08-27en
rioxxterms.versionofrecord10.1107/S2053230X15016076en
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2015-10-01en
dc.contributor.orcidMontgomery, Martin [0000-0001-6142-9423]
dc.contributor.orcidWalker, John [0000-0001-7929-2162]
dc.identifier.eissn2053-230X
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idMRC (MC_U105663150)


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International