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Science. 2017 Nov 17;358(6365):936-940. doi: 10.1126/science.aao4815. Epub 2017 Oct 26.

Atomic model for the dimeric FO region of mitochondrial ATP synthase.

Author information

1
Hospital for Sick Children Research Institute, Toronto, Ontario M5G 0A4, Canada.
2
Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
3
Hospital for Sick Children Research Institute, Toronto, Ontario M5G 0A4, Canada. john.rubinstein@utoronto.ca.
4
Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Abstract

Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded FO region turns the rotor that drives ATP synthesis in the soluble F1 region. Although crystal structures of the F1 region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the FO region. Using cryo-electron microscopy, we determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae.

PMID:
29074581
DOI:
10.1126/science.aao4815
[Indexed for MEDLINE]

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