Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
Article Details
- CitationCopy to clipboard
Menz RI, Walker JE, Leslie AG
Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
Cell. 2001 Aug 10;106(3):331-41.
- PubMed ID
- 11509182 [ View in PubMed]
- Abstract
The crystal structure of a novel aluminium fluoride inhibited form of bovine mitochondrial F(1)-ATPase has been determined at 2 A 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.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Aluminium Sodium/potassium-transporting ATPase subunit alpha-1 Protein Humans UnknownBinderDetails Aluminium phosphate Sodium/potassium-transporting ATPase subunit alpha-1 Protein Humans UnknownNot Available Details Aluminum acetate Sodium/potassium-transporting ATPase subunit alpha-1 Protein Humans UnknownNot Available Details