Proton translocation driven by ATP hydrolysis in V-ATPases - PubMed (original) (raw)
Review
. 2003 Jun 12;545(1):76-85.
doi: 10.1016/s0014-5793(03)00396-x.
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- PMID: 12788495
- DOI: 10.1016/s0014-5793(03)00396-x
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Review
Proton translocation driven by ATP hydrolysis in V-ATPases
Shoko Kawasaki-Nishi et al. FEBS Lett. 2003.
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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(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.
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