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TitleCryo-EM structure of the yeast ATP synthase.
Journal, issue, pagesJ Mol Biol, Vol. 382, Issue 5, Page 1256-1264, Year 2008
Publish dateOct 24, 2008
AuthorsWilson C Y Lau / Lindsay A Baker / John L Rubinstein /
PubMed AbstractWe have used electron cryomicroscopy of single particles to determine the structure of the ATP synthase from Saccharomyces cerevisiae. The resulting map at 24 A resolution can accommodate atomic ...We have used electron cryomicroscopy of single particles to determine the structure of the ATP synthase from Saccharomyces cerevisiae. The resulting map at 24 A resolution can accommodate atomic models of the F(1)-c(10) subcomplex, the peripheral stalk subcomplex, and the N-terminal domain of the oligomycin sensitivity conferral protein. The map is similar to an earlier electron cryomicroscopy structure of bovine mitochondrial ATP synthase but with important differences. It resolves the internal structure of the membrane region of the complex, especially the membrane embedded subunits b, c, and a. Comparison of the yeast ATP synthase map, which lacks density from the dimer-specific subunits e and g, with a map of the bovine enzyme that included e and g indicates where these subunits are located in the intact complex. This new map has allowed construction of a model of subunit arrangement in the F(O) motor of ATP synthase that dictates how dimerization of the complex via subunits e and g might occur.
External linksJ Mol Biol / PubMed:18722382
MethodsEM (single particle)
Resolution24.0 Å
Structure data

EMDB-2011:
Structure of the mitochondrial ATP synthase from Saccharomyces cerevisiae in Brij-35 at 24 Angstroms resolution.
Method: EM (single particle) / Resolution: 24.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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