PMID:10581164

Citation	Peña, HN, Vázquez-Contreras, E, de Gómez-Puyou, MT and Pérez-Hernández, G (1999) Nucleotide binding drives conformational changes in the isolated alpha and beta subunits of the F(1)-ATPase from Escherichia coli. Biochem. Biophys. Res. Commun. 266:58-61
Abstract	The modeling of the rotatory mechanism performed by the F(1)-ATPase complex during ATP synthesis shows that the beta, but not the alpha subunit, undergoes large conformational changes that depend on the occupancy of the catalytic site. Here we determined by fluorescence spectroscopy the changes in tertiary structure and hydrophobic exposed area of the isolated alpha and beta subunits of the F(1)-ATPase complex from Escherichia coli upon adenine nucleotide binding. The results show that in the absence of intersubunit contacts, the two subunits exhibit markedly similar conformational movements.
Links	PubMed Online version:10.1006/bbrc.1999.1770
Keywords	Adenine/metabolism; Anilino Naphthalenesulfonates/chemistry; Anilino Naphthalenesulfonates/metabolism; Escherichia coli/enzymology; Fluorescence; Fluorescent Dyes/chemistry; Fluorescent Dyes/metabolism; Magnesium/pharmacology; Nucleotides/metabolism; Protein Conformation/drug effects; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/metabolism; Solvents; Spectrometry, Fluorescence; Tryptophan/chemistry; Tryptophan/metabolism
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