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Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.

The proton pore of the F(1)F(o) ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c(10) ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release.

Pubmed ID: 22504883


  • Symersky J
  • Pagadala V
  • Osowski D
  • Krah A
  • Meier T
  • Faraldo-Gómez JD
  • Mueller DM


Nature structural & molecular biology

Publication Data

May 3, 2012

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM066223
  • Agency: NIGMS NIH HHS, Id: R01 GM066223-05
  • Agency: NIGMS NIH HHS, Id: R01 GM066223-06
  • Agency: NIGMS NIH HHS, Id: R01 GM066223-06S1
  • Agency: NIGMS NIH HHS, Id: R01 GM066223-06S2
  • Agency: NIGMS NIH HHS, Id: R01 GM066223-07
  • Agency: NIGMS NIH HHS, Id: R01 GM066223-08
  • Agency: NIGMS NIH HHS, Id: R01GM66223

Mesh Terms

  • Binding Sites
  • Crystallography, X-Ray
  • Mitochondrial Proton-Translocating ATPases
  • Molecular Dynamics Simulation
  • Protein Conformation
  • Protein Subunits
  • Protons
  • Saccharomyces cerevisiae