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Structural change and nucleotide dissociation of Myosin motor domain: dual go model simulation.

ABSTRACT: We investigated the structural relaxation of myosin motor domain from the pre-power stroke state to the near-rigor state using molecular dynamics simulation of a coarse-grained protein model. To describe the spontaneous structural change, we propose a dual G?-model-a variant of the G?-like model that has two reference structures. The nucleotide dissociation process is also studied by introducing a coarse-grained nucleotide in the simulation. We found that the myosin structural relaxation toward the near-rigor conformation cannot be completed before the nucleotide dissociation. Moreover, the relaxation and the dissociation occurred cooperatively when the nucleotide was tightly bound to the myosin head. The result suggested that the primary role of the nucleotide is to suppress the structural relaxation.

SUBMITTER: Takagi F

PROVIDER: S-EPMC2084243 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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Structural change and nucleotide dissociation of Myosin motor domain: dual go model simulation.

Takagi Fumiko F Kikuchi Macoto M

Biophysical journal 20070817 11

We investigated the structural relaxation of myosin motor domain from the pre-power stroke state to the near-rigor state using molecular dynamics simulation of a coarse-grained protein model. To describe the spontaneous structural change, we propose a dual Gō-model-a variant of the Gō-like model that has two reference structures. The nucleotide dissociation process is also studied by introducing a coarse-grained nucleotide in the simulation. We found that the myosin structural relaxation toward ...[more]

PMID: 17704146

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