Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.

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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

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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	Unknown	Binder	Details
Aluminium phosphate	Sodium/potassium-transporting ATPase subunit alpha-1	Protein	Humans	Unknown	Not Available	Details
Aluminum acetate	Sodium/potassium-transporting ATPase subunit alpha-1	Protein	Humans	Unknown	Not Available	Details