F(1)-ATPase: a prototypical rotary molecular motor.
F(1)-ATPase, the soluble portion of ATP synthase, has been shown to be a rotary molecular motor in which the central γ subunit rotates inside the cylinder made of α(3)β(3) subunits. The rotation is powered by ATP hydrolysis in three catalytic sites, and reverse rotation of the γ subunit by an external force leads to ATP synthesis in the catalytic sites. Here I look back how our lab became involved in the study of this marvelous rotary machine, and discuss some aspects of its rotary mechanism while confessing we are far from understanding. This article is a very personal essay, not a scientific review, for this otherwise viral machines book.
Department of Physics, Waseda University, Okubo, Shinjuku-ku, Tokyo, Japan. kazuhiko@waseda.jp
Kazuhiko
K
Kinosita
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry* / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*; D012399:Rotation; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism; D014780:Viruses / Q000201:enzymology*
D020409:Molecular Motor Proteins; D021122:Protein Subunits; D014764:Viral Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases