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Proton translocation driven by ATP hydrolysis in V-ATPases Kawasaki-Nishi S; Nishi T; Forgac MFEBS Lett 2003[Jun]; 545 (1): 76-85The 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(1)F(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.|*Protons[MESH]|Adenine Nucleotides/metabolism[MESH]|Adenosine Triphosphate/*metabolism[MESH]|Catalytic Domain[MESH]|Hydrolysis[MESH]|Ion Transport[MESH]|Models, Biological[MESH]|Protein Subunits[MESH]|Proton-Translocating ATPases/chemistry[MESH]|Vacuolar Proton-Translocating ATPases/*chemistry/*metabolism/ultrastructure[MESH] |
