The rotor in the membrane of the ATP synthase and relatives.
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.
Arechaga
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The Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, CB2 2XY, Cambridge, UK. ia@mrc-dunn.cam.ac.uk
Jones
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PC
D000255:Adenosine Triphosphate; D000595:Amino Acid Sequence; D000818:Animals; D002736:Chloroplasts / Q000201:enzymology; D006801:Humans; D006859:Hydrogen; D007477:Ions; D025261:Mitochondrial Proton-Translocating ATPases; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D025262:Vacuolar Proton-Translocating ATPases
D007477:Ions; D006859:Hydrogen; D000255:Adenosine Triphosphate; D025262:Vacuolar Proton-Translocating ATPases; C103607:mitochondrial ATPase subunit c; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases