The detachment kinetics from actin upon ATP binding is a key step in the reaction cycle of myosin V. We show that a network of residues, constituting the allostery wiring diagram (AWD), that trigger the rigor (R) to post-rigor (PR) transition, span key structural elements from the ATP and actin-binding regions. Several of the residues are in the 33 residue helix (H18), P loop, and switch I. Brownian dynamics simulations show that a hierarchy of kinetically controlled local structural changes leads to the opening of the " cleft" region, resulting in the detachment of the motor domain from actin. Movements in switch I and P loop facilitate changes in the rest of the motor domain, in particular the rotation of H18, whose stiffness within the motor domain is crucial in the R → PR transition. The finding that residues in the AWD also drive the kinetics of the R → PR transition shows how the myosin architecture regulates the allosteric movements during the reaction cycle. © 2010 Elsevier Ltd.
Tehver, R., & Thirumalai, D. (2010). Rigor to Post-Rigor Transition in Myosin V: Link between the Dynamics and the Supporting Architecture. Structure, 18(4), 471–481. https://doi.org/10.1016/j.str.2010.01.019