Mechanochemical coupling in the myosin motor domain. I. Insights from equilibrium active-site simulations.

ABSTRACT: Although the major structural transitions in molecular motors are often argued to couple to the binding of Adenosine triphosphate (ATP), the recovery stroke in the conventional myosin has been shown to be dependent on the hydrolysis of ATP. To obtain a clearer mechanistic picture for such "mechanochemical coupling" in myosin, equilibrium active-site simulations with explicit solvent have been carried out to probe the behavior of the motor domain as functions of the nucleotide chemical state and conformation of the converter/relay helix. In conjunction with previous studies of ATP hydrolysis with different active-site conformations and normal mode analysis of structural flexibility, the results help establish an energetics-based framework for understanding the mechanochemical coupling. It i

SUBMITTER: Yu H 

PROVIDER: S-EPMC1796662 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature