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Operating principles of rotary molecular motors: differences between F-1 and V-1 motors

Journal

BIOPHYSICS AND PHYSICOBIOLOGY
Volume 13, Issue -, Pages 37-44

Publisher

BIOPHYSICAL SOC JAPAN
DOI: 10.2142/biophysico.13.0_37

Keywords

V-ATPase; F-ATPase; ATP; Crystal structure; molecular mechanism

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Among the many types of bioenergy-transducing machineries, F-and V-ATPases are unique bio- and nano-molecular rotary motors. The rotational catalysis of F-1-ATPase has been investigated in detail, and molecular mechanisms have been proposed based on the crystal structures of the complex and on extensive single-molecule rotational observations. Recently, we obtained crystal structures of bacterial V-1-ATPase (A(3)B(3) and A(3)B(3)DF complexes) in the presence and absence of nucleotides. Based on these new structures, we present a novel model for the rotational catalysis mechanism of V-1-ATPase, which is different from that of F-1-ATPases.

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