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TitleStructure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution.
Journal, issue, pagesNat Struct Mol Biol, Vol. 19, Issue 12, Page 1356-1362, Year 2012
Publish dateNov 11, 2012
AuthorsSamir Benlekbir / Stephanie A Bueler / John L Rubinstein /
PubMed AbstractVacuolar-type ATPases (V-type ATPases) in eukaryotic cells are large membrane protein complexes that acidify various intracellular compartments. The enzymes are regulated by dissociation of the V(1) ...Vacuolar-type ATPases (V-type ATPases) in eukaryotic cells are large membrane protein complexes that acidify various intracellular compartments. The enzymes are regulated by dissociation of the V(1) and V(O) regions of the complex. Here we present the structure of the Saccharomyces cerevisiae V-type ATPase at 11-Å resolution by cryo-EM of protein particles in ice. The structure explains many cross-linking and protein interaction studies. Docking of crystal structures suggests that inhibition of ATPase activity by the dissociated V(1) region involves rearrangement of the N- and C-terminal domains of subunit H and also suggests how this inhibition is triggered upon dissociation. We provide support for this model by demonstrating that mutation of subunit H to increase the rigidity of the linker between its two domains decreases its ability to inhibit ATPase activity.
External linksNat Struct Mol Biol / PubMed:23142977
MethodsEM (single particle)
Resolution11.0 Å
Structure data

EMDB-5476:
Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11 Angstrom resolution
Method: EM (single particle) / Resolution: 11.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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