--- res: bibo_abstract: - The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the ‘proton translocation cluster’ attached to the c-ring and a more distant ‘hook apparatus’ holding subunit e. Unexpectedly, this subunit is anchored to a lipid ‘plug’ capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.@eng bibo_authorlist: - foaf_Person: foaf_givenName: Gergely foaf_name: Pinke, Gergely foaf_surname: Pinke foaf_workInfoHomepage: http://www.librecat.org/personId=4D5303E6-F248-11E8-B48F-1D18A9856A87 - foaf_Person: foaf_givenName: Long foaf_name: Zhou, Long foaf_surname: Zhou foaf_workInfoHomepage: http://www.librecat.org/personId=3E751364-F248-11E8-B48F-1D18A9856A87 orcid: 0000-0002-1864-8951 - foaf_Person: foaf_givenName: Leonid A foaf_name: Sazanov, Leonid A foaf_surname: Sazanov foaf_workInfoHomepage: http://www.librecat.org/personId=338D39FE-F248-11E8-B48F-1D18A9856A87 orcid: 0000-0002-0977-7989 bibo_doi: 10.1038/s41594-020-0503-8 bibo_issue: '11' bibo_volume: 27 dct_date: 2020^xs_gYear dct_identifier: - UT:000569299400004 dct_isPartOf: - http://id.crossref.org/issn/15459993 - http://id.crossref.org/issn/15459985 dct_language: eng dct_publisher: Springer Nature@ dct_title: Cryo-EM structure of the entire mammalian F-type ATP synthase@ fabio_hasPubmedId: '32929284' ...