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dc.contributor.authorZhou, Annaen
dc.contributor.authorRohou, Alexisen
dc.contributor.authorSchep, Daniel Gen
dc.contributor.authorBason, John Ven
dc.contributor.authorMontgomery, Martinen
dc.contributor.authorWalker, Johnen
dc.contributor.authorGrigorieff, Nikolausen
dc.contributor.authorRubinstein, John Len
dc.date.accessioned2017-08-09T09:01:19Z
dc.date.available2017-08-09T09:01:19Z
dc.date.issued2015-10-06en
dc.identifier.issn2050-084X
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/266076
dc.description.abstractAdenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted FO region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the FO region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the FO region support a Brownian ratchet mechanism for proton-translocation-driven rotation in ATP synthases.
dc.languageengen
dc.rightsAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectATP synthaseen
dc.subjectbiochemistryen
dc.subjectbiophysicsen
dc.subjectbovineen
dc.subjectcoevolutionen
dc.subjectcryo-EMen
dc.subjectevolutionary covarianceen
dc.subjectstructural biologyen
dc.subjectstructureen
dc.subjectAnimalsen
dc.subjectCattleen
dc.subjectComputational Biologyen
dc.subjectCryoelectron Microscopyen
dc.subjectImaging, Three-Dimensionalen
dc.subjectMitochondrial Proton-Translocating ATPasesen
dc.subjectModels, Molecularen
dc.subjectProtein Conformationen
dc.subjectProtein Foldingen
dc.titleStructure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.en
dc.typeArticle
prism.numbere10180en
prism.publicationDate2015en
prism.publicationNameElifeen
prism.volume4en
dc.identifier.doi10.17863/CAM.9968
dcterms.dateAccepted2015-10-05en
rioxxterms.versionofrecord10.7554/eLife.10180en
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2015-10-06en
dc.contributor.orcidMontgomery, Martin [0000-0001-6142-9423]
dc.contributor.orcidWalker, John [0000-0001-7929-2162]
dc.identifier.eissn2050-084X
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idMRC (MC_EX_MR/M009858/1)
pubs.funder-project-idMRC (MC_U105663150)
dc.identifier.urlhttps://elifesciences.org/articles/10180en


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