F- and V-ATPases are unique bio- and nano-molecular rotary motors among many types of bioenergy-transducing machineries. The rotational catalysis of F
1-ATPase has been investigated in detail, and the molecular mechanisms have been proposed on the basis of crystal structures of the complex and extensive single-molecule observation of the rotation. Recently, we have obtained crystal structures of bacterial V
1-ATPase (A
3B
3 and A
3B
3DF complexes) with and without nucleotide. On the basis of these new structures, we present a novel model of the rotational catalytic mechanism for V
1-ATPase, which is apparently different from those of F
1-ATPases.
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