Journal
CELL
Volume 106, Issue 3, Pages 331-341Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(01)00452-4
Keywords
-
Categories
Ask authors/readers for more resources
The crystal structure of a novel aluminium fluoride inhibited form of bovine mitochondrial F-1-ATPase has been determined at 2 Angstrom resolution. In contrast to all previously determined structures of the bovine enzyme, all three catalytic sites are occupied by nucleotide. The subunit that did not bind nucleotide in previous structures binds ADP and sulfate (mimicking phosphate), and adopts a half-closed conformation. This structure probably represents the posthydrolysis, pre-product release step on the catalytic pathway. A catalytic scheme for hydrolysis (and synthesis) at physiological rates and a mechanism for the ATP-driven rotation of the gamma subunit are proposed based on the crystal structures of the bovine enzyme.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available