Atomic model for the dimeric F O region of mitochondrial ATP synthase

Author:

Guo Hui12ORCID,Bueler Stephanie A.1,Rubinstein John L.123ORCID

Affiliation:

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. Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Abstract

How protons power rotation Synthesis of adenosine triphosphate (ATP) in mitochondria is accomplished by a large molecular machine, the F 1 F O ATP synthase. Proton translocation across the F O region that spans the mitochondrial inner membrane drives ATP synthesis in the F 1 region through a rotational mechanism. Guo et al. present a high-resolution structure of the dimeric F O complex from Saccharomyces cerevisiae , determined by electron microscopy. The structure gives insights into how proton translocation powers rotation and suggests how F O dimers bend the membrane to give mitochondria their characteristic cristae. Science , this issue p. 936

Funder

National Institutes of Health

Simons Foundation

Canadian Institutes of Health Research

Canada Research Chairs

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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