Abstract
The vacuolar H +-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are multisubunit complexes composed of a peripheral domain (V 1) responsible for ATP hydrolysis and an integral domain (V 0) responsible for proton translocation. Based upon their structural similarity to the F 1F 0 ATP synthases, the V-ATPases are thought to operate by a rotary mechanism in which ATP hydrolysis in V 1 drives rotation of a ring of proteolipid subunits in V 0. This review is focused on the current structural knowledge of the V-ATPases as it relates to the mechanism of ATP-driven proton translocation.
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