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Reference: Hahn, Alexander, Parey, Kristian, Bublitz, Maike et al., (2016). Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology. Molecular Cell, 63 (3), 445-456.Citable link to this page:

 

Structure of a complete ATP synthase dimer reveals the molecular basis of inner mitochondrial membrane morphology

Abstract: We determined the structure of a complete, dimeric F1Fo-ATP synthase from yeast Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The final structure resolves 58 of the 60 dimer subunits. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Subunit 8 (A6L in human) is an evolutionary derivative of the bacterial b subunit. On the lumenal membrane surface, subunit f establishes direct contact between the two monomers. Comparison with a cryo-EM map of the F1Fo monomer identifies subunits e and g at the lateral dimer interface. They do not form dimer contacts but enable dimer formation by inducing a strong membrane curvature of ∼100°. Our structure explains the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology. ATP synthases are complex macromolecular machines that supply most of the ATP in cells. Hahn et al. present the structure of a complete ATP synthase dimer, which provides insights into both the mechanism of these nanomotors and how they cause membrane bending to form cristae in the inner mitochondrial membrane.

Publication status:PublishedPeer Review status:Peer reviewedVersion:Publisher's VersionDate of acceptance:2016-05-26 Funder: Wellcome Trust   Funder: Max-Planck Society   Funder: Deutsche Forschungsgemeinschaft   Funder: Cluster of Excellence Frankfurt "Macromolecular Complexes"   Notes:© 2016 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/)

Bibliographic Details

Publisher: Elsevier

Publisher Website: https://www.elsevier.com/

Journal: Molecular Cellsee more from them

Publication Website: http://www.cell.com/molecular-cell/home

Volume: 63

Issue Date: 2016-08-04

pages:445-456Identifiers

Issn: 1097-2765

Eissn: 1097-4164

Uuid: uuid:5c0e6fa9-8e61-498c-a744-767e40587fc0

Urn: uri:5c0e6fa9-8e61-498c-a744-767e40587fc0

Pubs-id: pubs:637595

Doi: https://doi.org/10.1016/j.molcel.2016.05.037 Item Description

Type: journal-article;

Version: Publisher's VersionKeywords: mitochondria inner membrane morphology F1Fo-ATP synthase dimer bioenergetics membrane protein complex rotary ATPase mechanism yeast Yarrowia lipolyticar cryoelectron microscopy X-ray crystallography

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Author: Hahn, Alexander - - - Parey, Kristian - - - Bublitz, Maike - Oxford, MSD, Biochemistry - - - Mills, Deryck J. - - - Zickermann, V

Source: https://ora.ox.ac.uk/objects/uuid:5c0e6fa9-8e61-498c-a744-767e40587fc0



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