The rotor in the membrane of the ATP synthase and relatives

FEBS Letters
I Arechaga, P C Jones

Abstract

In recent years, structural information on the F(1) sector of the ATP synthase has provided an insight into the molecular mechanism of ATP catalysis. The structure strongly supports the proposal that the ATP synthase works as a rotary molecular motor. Insights into the membrane domain have just started to emerge but more detailed structural information is needed if the molecular mechanism of proton translocation coupled to ATP synthesis is to be understood. This review will focus mainly on the ion translocating rotor in the membrane domain of the F-type ATPase, and the related vacuolar and archaeal relatives.

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Feb 20, 2003·Journal of Bacteriology·Wendi L Kuhnert, Robert G Quivey
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Related Concepts

Mitochondrial ATPase subunit c
Striadyne
Metazoa
Etioplasts
H(+)-Transporting ATP Synthase, Acyl-Phosphate-Linked
Hydrogen
Ions
Saccharomyces cerevisiae
Mitochondrial Proton-Translocating ATPases
Vacuolar H+-ATPase

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