Atomic model for the membrane-embedded V_O motor of a eukaryotic V-ATPase.

ABSTRACT: 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 V₁ region drives proton translocation through the membrane-embedded V_O 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 V₁ and V_O 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_O complex and build atomic m

SUBMITTER: Mazhab-Jafari MT 

PROVIDER: S-EPMC7332345 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature