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Proton translocation driven by ATP hydrolysis in V‐ATPases
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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 (V1) responsible for ATP hydrolysis and an integral domain (V0) responsible for proton translocation. Based upon their structural similarity to the F1F0 ATP synthases, the V‐ATPases are thought to operate by a rotary mechanism in which ATP hydrolysis in V1 drives rotation of a ring of proteolipid subunits in V0. This review is focused on the current structural knowledge of the V‐ATPases as it relates to the mechanism of ATP‐driven proton translocation.
Title: Proton translocation driven by ATP hydrolysis in V‐ATPases
Description:
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 (V1) responsible for ATP hydrolysis and an integral domain (V0) responsible for proton translocation.
Based upon their structural similarity to the F1F0 ATP synthases, the V‐ATPases are thought to operate by a rotary mechanism in which ATP hydrolysis in V1 drives rotation of a ring of proteolipid subunits in V0.
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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