Characterization of the pre-force-generation state in the actomyosin cross-bridge cycle.

ABSTRACT: Myosin is an actin-based motor protein that generates force by cycling between actin-attached (strong binding: ADP or rigor) and actin-detached (weak binding: ATP or ADP.P(i)) states during its ATPase cycle. However, it remains unclear what specific conformational changes in the actin binding site take place on binding to actin, and how these structural changes lead to product release and the production of force and motion. We studied the dynamics of the actin binding region of myosin V by using fluorescence resonance energy transfer (FRET) to monitor conformational changes in the upper-50-kDa domain of the actin binding cleft in the weak and strong actin binding states. Steady-state and lifetime data monitoring the FRET signal suggest that the cleft is in a more open conformation in the w

SUBMITTER: Sun M 

PROVIDER: S-EPMC2438420 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature