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Atomic model for the dimeric FO region of mitochondrial ATP synthase

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Science  26 Oct 2017:
eaao4815
DOI: 10.1126/science.aao4815

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Abstract

Mitochondrial 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. While crystal structures of the F1 region have illustrated how rotation leads to ATP synthesis, the lack of an experimental atomic model for the FO region has prevented understanding how proton translocation produces rotation. We determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at 3.6 Å resolution by electron cryomicroscopy. The structure reveals the proton path through the complex, how the complex dimerizes, and suggests how it bends the membrane to produce cristae.

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