Structural change and nucleotide dissociation of Myosin motor domain: dual go model simulation.
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 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.
Takagi
Fumiko
F
Formation of Soft Nanomachines, Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Osaka, Japan. fumiko@cp.cmc.osaka-u.ac.jp
Kikuchi
Macoto
M
D000255:Adenosine Triphosphate / Q000737:chemistry*; D001665:Binding Sites; D004735:Energy Transfer; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D009038:Motion; D009218:Myosins / Q000737:chemistry* / Q000648:ultrastructure*; D009711:Nucleotides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical; D013329:Structure-Activity Relationship
D020409:Molecular Motor Proteins; D009711:Nucleotides; D000255:Adenosine Triphosphate; D009218:Myosins
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