Extensive conformational transitions are required to turn on ATP hydrolysis in myosin.

ABSTRACT: Conventional myosin is representative of biomolecular motors in which the hydrolysis of adenosine triphosphate (ATP) is coupled to large-scale structural transitions both in and remote from the active site. The mechanism that underlies such "mechanochemical coupling," especially the causal relationship between hydrolysis and allosteric structural changes, has remained elusive despite extensive experimental and computational analyses. In this study, using combined quantum mechanical and molecular mechanical simulations and different conformations of the myosin motor domain, we provide evidence to support that regulation of ATP hydrolysis activity is not limited to residues in the immediate environment of the phosphate. Specifically, we illustrate that efficient hydrolysis of ATP depends not

SUBMITTER: Yang Y 

PROVIDER: S-EPMC2756066 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature