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

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Mitochondria / enzymology
  • Mitochondrial Proton-Translocating ATPases / chemistry*
  • Models, Molecular*
  • Protein Folding
  • Protein Multimerization
  • Protein Structure, Secondary
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*

Substances

  • Saccharomyces cerevisiae Proteins
  • Mitochondrial Proton-Translocating ATPases