Abstract
In the F1-ATPase complex, the conformational change of the catalytically active β subunit is propagated to the entire α3β3 ring, resulting in an asymmetry in the hexamer. With the sequential nucleotide perturbations, the asymmetrical α3β3 structure changes from one state to the other, which rotates the γ subunit axis. Basically, the two elements: the β structural change and the asymmetrical α3β3 are essential for the molecular motor rotation. Therefore, we have been studying them using molecular dynamics (MD) simulations. The results in a series of our studies deepen the understanding of the rotational mechanism of the motor.
