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

TitleStructure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis.
Publication TypeJournal Article
Year of Publication2001
AuthorsMenz, RI, Walker, JE, Leslie, AG
JournalCell
Volume106
Issue3
Pagination331-41
Date Published2001 Aug 10
ISSN0092-8674
KeywordsAdenosine Diphosphate, Adenosine Triphosphate, Allosteric Regulation, Aluminum Compounds, Animals, Binding Sites, Catalysis, Cattle, Crystallography, X-Ray, Enzyme Inhibitors, Fluorides, Hydrolysis, Mitochondria, Models, Biological, Models, Molecular, Nucleotides, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, Proton-Translocating ATPases, Rotation, Structure-Activity Relationship, Sulfates
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.

DOI10.1016/s0092-8674(01)00452-4
Alternate JournalCell
Citation Key10.1016/s0092-8674(01)00452-4
PubMed ID11509182