期刊
STRUCTURE
卷 18, 期 4, 页码 471-481出版社
CELL PRESS
DOI: 10.1016/j.str.2010.01.019
关键词
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资金
- National Institute of General Medical Sciences [1 F32GM082009]
- National Science Foundation [CHE 09-14033]
- National Institutes of Health
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [0910433] Funding Source: National Science Foundation
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 -> R transition shows how the myosin architecture regulates the allosteric movements during the reaction cycle.
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