| Literature DB >> 10093703 |
A G Leslie1, J P Abrahams, K Braig, R Lutter, R I Menz, G L Orriss, M J van Raaij, J E Walker.
Abstract
There is now compelling evidence in support of a rotary catalytic mechanism in F1-ATPase, and, by extension, in the intact ATP synthase. Although models have been proposed to explain how protein translocation in F0 results in rotation of the gamma-subunit relative to the alpha 3/beta 3 assembly in F1 [22], these are still speculative. It seems likely that a satisfactory explanation of this mechanism will ultimately depend on structural information on the intact ATP synthase.Entities:
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Year: 1999 PMID: 10093703 DOI: 10.1042/bst0270037
Source DB: PubMed Journal: Biochem Soc Trans ISSN: 0300-5127 Impact factor: 5.407