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The rotor in the membrane of the ATP synthase and relatives Arechaga I; Jones PCFEBS Lett 2001[Apr]; 494 (1-2): 1-5In 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.|*Mitochondrial Proton-Translocating ATPases[MESH]|*Vacuolar Proton-Translocating ATPases[MESH]|Adenosine Triphosphate[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Chloroplasts/enzymology[MESH]|Humans[MESH]|Hydrogen[MESH]|Ions[MESH]|Molecular Sequence Data[MESH]|Proton-Translocating ATPases/*chemistry[MESH]|Saccharomyces cerevisiae/enzymology[MESH] |
