Structural Change of Myosin Motor Domain and Nucleotide Dissociation

Details Structural Change of Myosin Motor Domain and Nucleotide Dissociation Structural Change of Myosin Motor Domain and Nucleotide Dissociation

2006-05-19

arxiv.org/abs/q-bio/0605031v2

Biology

Quantitative Biology

Biomolecules

Scientific paper

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 structural change, we propose a "dual Go-model," a variant of the Go-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.

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