Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution.

TitleGround state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution.
Publication TypeJournal Article
Year of Publication2007
AuthorsBowler, MW, Montgomery, MG, Leslie, AGW, Walker, JE
JournalJ Biol Chem
Date Published2007 May 11
KeywordsAdenosine Diphosphate, Adenylyl Imidodiphosphate, Animals, Azides, Binding Sites, Catalytic Domain, Cattle, Crystallization, Crystallography, X-Ray, Hydrolysis, Mitochondria, Heart, Models, Molecular, Protein Conformation, Proton-Translocating ATPases

The structure of bovine F(1)-ATPase, crystallized in the presence of AMP-PNP and ADP, but in the absence of azide, has been determined at 1.9A resolution. This structure has been compared with the previously described structure of bovine F(1)-ATPase determined at 1.95A resolution with crystals grown under the same conditions but in the presence of azide. The two structures are extremely similar, but they differ in the nucleotides that are bound to the catalytic site in the beta(DP)-subunit. In the present structure, the nucleotide binding sites in the beta(DP)- and beta(TP)-subunits are both occupied by AMP-PNP, whereas in the earlier structure, the beta(TP) site was occupied by AMP-PNP and the beta(DP) site by ADP, where its binding is enhanced by a bound azide ion. Also, the conformation of the side chain of the catalytically important residue, alphaArg-373 differs in the beta(DP)- and beta(TP)-subunits. Thus, the structure with bound azide represents the ADP inhibited state of the enzyme, and the new structure represents a ground state intermediate in the active catalytic cycle of ATP hydrolysis.

Alternate JournalJ. Biol. Chem.
Citation Key10.1074/jbc.M700203200
PubMed ID17350959
Grant ListMC_U105184325 / / Medical Research Council / United Kingdom
MC_U105663150 / / Medical Research Council / United Kingdom