Molecular switch of F0F1-ATP synthase, G-protein, and other ATP-driven enzymes.
Exchange-out of amide tritium from labeled gamma-subunit of alpha 3 beta 3 gamma complex of F0F1-ATP synthase was not accelerated by ATP, suggesting that hemagglutinin-type transition of coiled-coil structure did not occur in gamma-subunit. Local topology of nucleotide binding site and "switch II" region of G-protein alpha resemble those of F1-beta subunit and other proteins which catalyze ATP-triggered reactions. Probably, binding of nucleotide to F0F1-ATP synthase induces conformational change of the switch II-like region with transforming beta subunit structure from "open" to "close" for and this transformation results in loss of hydrogen bonds with gamma subunit, thus enabling the gamma subunit to move.
Noji
H
H
Research laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Amano
T
T
Yoshida
M
M
D000255:Adenosine Triphosphate / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism*
D000255:Adenosine Triphosphate; D019204:GTP-Binding Proteins; D006180:Proton-Translocating ATPases