The rotor in the membrane of the ATP synthase and relatives
Copyright policy )The rotor in the membrane of the ATP synthase and relatives
In recent years, structural information on the F1 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.
- Wellcome Trust United Kingdom
Ions, Vacuolar Proton-Translocating ATPases, Chloroplasts, Molecular Sequence Data, Subunit c, Proton stoichiometry, Saccharomyces cerevisiae, Mitochondrial Proton-Translocating ATPases, Proton-Translocating ATPases, Adenosine Triphosphate, Sequence alignment, ATP synthase, Animals, Humans, Amino Acid Sequence, Hydrogen
Ions, Vacuolar Proton-Translocating ATPases, Chloroplasts, Molecular Sequence Data, Subunit c, Proton stoichiometry, Saccharomyces cerevisiae, Mitochondrial Proton-Translocating ATPases, Proton-Translocating ATPases, Adenosine Triphosphate, Sequence alignment, ATP synthase, Animals, Humans, Amino Acid Sequence, Hydrogen
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