Folding-based molecular simulations reveal mechanisms of the rotary motor F1-ATPase.

ABSTRACT: Biomolecular machines fulfill their function through large conformational changes that typically occur on the millisecond time scale or longer. Conventional atomistic simulations can only reach microseconds at the moment. Here, extending the minimalist model developed for protein folding, we propose the "switching Gō model" and use it to simulate the rotary motion of ATP-driven molecular motor F(1)-ATPase. The simulation recovers the unidirectional 120 degrees rotation of the gamma-subunit, the rotor. The rotation was induced solely by steric repulsion from the alpha(3)beta(3) subunits, the stator, which undergoes conformation changes during ATP hydrolysis. In silico alanine mutagenesis further elucidated which residues play specific roles in the rotation. Finally, regarding the mechanoche

SUBMITTER: Koga N 

PROVIDER: S-EPMC1459361 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature