Nucleotide binding drives conformational changes in the isolated alpha and beta subunits of the F(1)-ATPase from Escherichia coli.
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.
Peña
H N
HN
Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, México.
Vázquez-Contreras
E
E
de Gómez-Puyou
M T
MT
Pérez-Hernández
G
G
D000225:Adenine / Q000378:metabolism; D000817:Anilino Naphthalenesulfonates / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005453:Fluorescence; D005456:Fluorescent Dyes / Q000737:chemistry / Q000378:metabolism; D008274:Magnesium / Q000494:pharmacology; D009711:Nucleotides / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D012997:Solvents; D013050:Spectrometry, Fluorescence; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism
D000817:Anilino Naphthalenesulfonates; D005456:Fluorescent Dyes; D009711:Nucleotides; D012997:Solvents; C027132:1-anilino-8-naphthalenesulfonate; D014364:Tryptophan; D006180:Proton-Translocating ATPases; D008274:Magnesium; D000225:Adenine