Atomic model for the dimeric FO region of mitochondrial ATP synthase

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Science  17 Nov 2017:
Vol. 358, Issue 6365, pp. 936-940
DOI: 10.1126/science.aao4815

How protons power rotation

Synthesis of adenosine triphosphate (ATP) in mitochondria is accomplished by a large molecular machine, the F1FO ATP synthase. Proton translocation across the FO region that spans the mitochondrial inner membrane drives ATP synthesis in the F1 region through a rotational mechanism. Guo et al. present a high-resolution structure of the dimeric FO complex from Saccharomyces cerevisiae, determined by electron microscopy. The structure gives insights into how proton translocation powers rotation and suggests how FO dimers bend the membrane to give mitochondria their characteristic cristae.

Science, this issue p. 936


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.

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