The alpha 3 beta 3 and alpha 1 beta 1 complexes of ATP synthase.
Two catalytic structures of H(+)-motive ATP synthase (Fig. 1), the alpha 3 beta 3 oligomer (M(r) = 319,581) and alpha 1 beta 1 promoter (M(r) = 106,527) (Fig. 2), were isolated using high pressure liquid chromatography (Fig. 3) and polyacrylamide gel electrophoresis (Figs. 4 and 5). These were reconstituted from the alpha and beta subunits of thermophilic F1 (TF1), and the alpha 3 beta 3 oligomer was also crystallized. Common to both F1 and the alpha 3 beta 3 oligomer were the nucleotide specificity, the two Km values, the presence of protomer-oligomer activities, and the one-hit--one-kill phenomenon. A synchrotron experiment on the ATP hydrolysis cycle revealed the dynamic shrinkage and expansion of F1(44) that correspond, respectively, to the ATP-induced association and ADP-induced dissociation of the alpha 3 beta 3 oligomer. The oligomer, like mitochondrial F1 and TF1, exhibited two kinds of ATPase activity: one was cooperative and was inhibited by only one inhibitor per hexamer, and the other was inhibited by three inhibitors per hexamer.
Kagawa
Y
Y
Department of Biochemistry, Jichi Medical School, Tochigi, Japan.
Ohta
S
S
Harada
M
M
Sato
M
M
Itoh
Y
Y
D000255:Adenosine Triphosphate / Q000378:metabolism; D000494:Allosteric Regulation; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers; D046911:Macromolecular Substances; D008954:Models, Biological; D008961:Models, Structural; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D017356:Synchrotrons
D008051:Lipid Bilayers; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases