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

AUTOR(ES)

Kagawa, Reiko

RESUMO

The structure of bovine F1-ATPase inhibited with ADP and beryllium fluoride at 2.0 Å resolution contains two ADP.BeF3− complexes mimicking ATP, bound in the catalytic sites of the βTP and βDP subunits. Except for a 1 Å shift in the guanidinium of αArg373, the conformations of catalytic side chains are very similar in both sites. However, the ordered water molecule that carries out nucleophilic attack on the γ-phosphate of ATP during hydrolysis is 2.6 Å from the beryllium in the βDP subunit and 3.8 Å away in the βTP subunit, strongly indicating that the βDP subunit is the catalytically active conformation. In the structure of F1-ATPase with five bound ADP molecules (three in α-subunits, one each in the βTP and βDP subunits), which has also been determined, the conformation of αArg373 suggests that it senses the presence (or absence) of the γ-phosphate of ATP. Two catalytic schemes are discussed concerning the various structures of bovine F1-ATPase.

Documentos Relacionados

• The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin.
• The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B.
• The missing link between thermodynamics and structure in F1-ATPase
• Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 A resolution.
• Structure of spinach chloroplast F1-ATPase complexed with the phytopathogenic inhibitor tentoxin