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TitleAtomic model for the membrane-embedded V motor of a eukaryotic V-ATPase.
Journal, issue, pagesNature, Vol. 539, Issue 7627, Page 118-122, Year 2016
Publish dateNov 3, 2016
AuthorsMohammad T Mazhab-Jafari / Alexis Rohou / Carla Schmidt / Stephanie A Bueler / Samir Benlekbir / Carol V Robinson / John L Rubinstein /
PubMed AbstractVacuolar-type ATPases (V-ATPases) are ATP-powered proton pumps involved in processes such as endocytosis, lysosomal degradation, secondary transport, TOR signalling, and osteoclast and kidney ...Vacuolar-type ATPases (V-ATPases) are ATP-powered proton pumps involved in processes such as endocytosis, lysosomal degradation, secondary transport, TOR signalling, and osteoclast and kidney function. ATP hydrolysis in the soluble catalytic V region drives proton translocation through the membrane-embedded V region via rotation of a rotor subcomplex. Variability in the structure of the intact enzyme has prevented construction of an atomic model for the membrane-embedded motor of any rotary ATPase. We induced dissociation and auto-inhibition of the V and V regions of the V-ATPase by starving the yeast Saccharomyces cerevisiae, allowing us to obtain a ~3.9-Å resolution electron cryomicroscopy map of the V complex and build atomic models for the majority of its subunits. The analysis reveals the structures of subunits acc'c″de and a protein that we identify and propose to be a new subunit (subunit f). A large cavity between subunit a and the c-ring creates a cytoplasmic half-channel for protons. The c-ring has an asymmetric distribution of proton-carrying Glu residues, with the Glu residue of subunit c″ interacting with Arg735 of subunit a. The structure suggests sequential protonation and deprotonation of the c-ring, with ATP-hydrolysis-driven rotation causing protonation of a Glu residue at the cytoplasmic half-channel and subsequent deprotonation of a Glu residue at a luminal half-channel.
External linksNature / PubMed:27776355 / PubMed Central
MethodsEM (single particle)
Resolution3.9 - 8.7 Å
Structure data

EMDB-8363:
CryoEM map of the S. cerevisiae Vo region lacking subunit d
Method: EM (single particle) / Resolution: 7.8 Å

EMDB-8364:
CryoEM map of the S. cerevisiae Vo region solubilized in DDM
Method: EM (single particle) / Resolution: 8.3 Å

EMDB-8367:
CryoEM map of the Vo region from S. cerevisiae yeast strain with the open reading frame YPR170W-B deleted
Method: EM (single particle) / Resolution: 8.7 Å

8409

5tj5

EMDB-8409, PDB-5tj5:
Atomic model for the membrane-embedded motor of a eukaryotic V-ATPase
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsMOTOR PROTEIN / Rotary ATPase / Vacuolar-type ATPase / Electron Cryomicroscopy / Vo region / Membrane protein

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