Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex.

@article{Oot2012CrystalSO,
  title={Crystal structure of the yeast vacuolar ATPase heterotrimeric EGC(head) peripheral stalk complex.},
  author={Rebecca A Oot and Li-shar Huang and Edward A Berry and Stephan Wilkens},
  journal={Structure},
  year={2012},
  volume={20 11},
  pages={1881-92}
}
Vacuolar ATPases (V-ATPases) are multisubunit rotary motor proton pumps that function to acidify subcellular organelles in all eukaryotic organisms. V-ATPase is regulated by a unique mechanism that involves reversible dissociation into V₁-ATPase and V₀ proton channel, a process that involves breaking of protein interactions mediated by subunit C, the cytoplasmic domain of subunit "a" and three "peripheral stalks," each made of a heterodimer of E and G subunits. Here, we present crystal… CONTINUE READING
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