|Title||The rotor in the membrane of the ATP synthase and relatives.|
|Publication Type||Journal Article|
|Year of Publication||2001|
|Authors||Arechaga, I, Jones, PC|
|Date Published||2001 Apr 06|
|Keywords||Adenosine Triphosphate, Amino Acid Sequence, Animals, Chloroplasts, Humans, Hydrogen, Ions, Mitochondrial Proton-Translocating ATPases, Molecular Sequence Data, Proton-Translocating ATPases, Saccharomyces cerevisiae, Vacuolar Proton-Translocating ATPases|
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.
|Alternate Journal||FEBS Lett.|