Dynamic conformational changes due to the ATP hydrolysis in the motor domain of myosin: 10-ns molecular dynamics simulations.
Muscle contraction is caused by directed movement of myosin heads along actin filaments. This movement is triggered by ATP hydrolysis, which occurs within the motor domain of myosin. The mechanism for this intramolecular process remains unknown owing to a lack of ways to observe the detailed motions of each atom in the myosin molecule. We carried out 10-ns all-atom molecular dynamics simulations to investigate the types of dynamic conformational changes produced in the motor domain by the energy released from ATP hydrolysis. The results revealed that the thermal fluctuations modulated by perturbation of ATP hydrolysis are biased in one direction that is relevant to directed movement of the myosin head along the actin filament.
Kawakubo
Tatsuyuki
T
Toin University of Yokohama, Aoba-ku, Japan. tatsu@cc.toin.ac.jp
Okada
Okimasa
O
Minami
Tomoyuki
T
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002244:Carbon; D004023:Dictyostelium; D006868:Hydrolysis; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D013997:Time Factors
D015800:Protozoan Proteins; D002244:Carbon; D000255:Adenosine Triphosphate; D009218:Myosins