The structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride.

TitleThe structure of bovine F1-ATPase inhibited by ADP and beryllium fluoride.
Publication TypeJournal Article
Year of Publication2004
AuthorsKagawa, R, Montgomery, MG, Braig, K, Leslie, AGW, Walker, JE
JournalEMBO J
Date Published2004 Jul 21
KeywordsAdenosine Diphosphate, Animals, Arginine, Beryllium, Binding Sites, Catalytic Domain, Cattle, Crystallography, X-Ray, Enzyme Inhibitors, Fluorides, Hydrolysis, Models, Molecular, Protein Binding, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary, Proton-Translocating ATPases, Water

The structure of bovine F1-ATPase inhibited with ADP and beryllium fluoride at 2.0 angstroms resolution contains two ADP.BeF3- complexes mimicking ATP, bound in the catalytic sites of the beta(TP) and beta(DP) subunits. Except for a 1 angstrom shift in the guanidinium of alphaArg373, the conformations of catalytic side chains are very similar in both sites. However, the ordered water molecule that carries out nucleophilic attack on the gamma-phosphate of ATP during hydrolysis is 2.6 angstroms from the beryllium in the beta(DP) subunit and 3.8 angstroms away in the beta(TP) subunit, strongly indicating that the beta(DP) subunit is the catalytically active conformation. In the structure of F1-ATPase with five bound ADP molecules (three in alpha-subunits, one each in the beta(TP) and beta(DP) subunits), which has also been determined, the conformation of alphaArg373 suggests that it senses the presence (or absence) of the gamma-phosphate of ATP. Two catalytic schemes are discussed concerning the various structures of bovine F1-ATPase.

Alternate JournalEMBO J.
Citation Key10.1038/sj.emboj.7600293
PubMed ID15229653
PubMed Central IDPMC514953