title: Cryo-EM structures of the autoinhibitedE. coliATP synthase in three rotational states.
abstract: A molecular model that provides a framework for interpreting the wealth of functional information obtained on theE. coliF-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk's ε subunit in an extended autoinhibitory conformation in all three states. The Fomotor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F1attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunitafrom two sides.
authors.affiliation: Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.
authors.forename: Meghna
authors.initials: M
authors.lastname: Sobti
authors.affiliation: Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.
authors.forename: Callum
authors.initials: C
authors.lastname: Smits
authors.affiliation: NTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore.
authors.forename: Andrew Sw
authors.initials: AS
authors.lastname: Wong
authors.affiliation: Department of Physics, Clarendon Laboratory, University of Oxford, Oxford, United Kingdom.
authors.forename: Robert
authors.initials: R
authors.lastname: Ishmukhametov
authors.affiliation: Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.|Faculty of Medicine, The University of New South Wales, Sydney, Australia.
authors.forename: Daniela
authors.initials: D
authors.lastname: Stock
authors.affiliation: NTU Institute of Structural Biology, Nanyang Technological University, Singapore, Singapore.|School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
authors.forename: Sara
authors.initials: S
authors.lastname: Sandin
authors.affiliation: Molecular, Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Darlinghurst, Australia.|Faculty of Medicine, The University of New South Wales, Sydney, Australia.
authors.forename: Alastair G
authors.identifier: 0000-0002-2070-6030
authors.initials: AG
authors.lastname: Stewart
mesh_terms: D025243:Bacterial Proton-Translocating ATPases / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D004926:Escherichia coli / Q000201:enzymology*
chemical_list: D025243:Bacterial Proton-Translocating ATPases
keywords: ATP synthase; E. coli; bioenergetics; biophysics; cryoEM; membrane protein; rotary ATPase; structural biology