Dielectric Allostery of Protein: Response of Myosin to ATP Binding

Takato Sato, Jun Ohnuki, Mitsunori Takano*

*この研究の対応する著者

研究成果: Article査読

12 被引用数 (Scopus)

抄録

Protein uses allostery to execute biological function. The physical mechanism underlying the allostery has long been studied, with the focus on the mechanical response by ligand binding. Here, we highlight the electrostatic response, presenting an idea of "dielectric allostery". We conducted molecular dynamics simulations of myosin, a motor protein with allostery, and analyzed the response to ATP binding which is a crucial step in force-generating function, forcing myosin to unbind from the actin filament. We found that the net negative charge of ATP causes a large-scale, anisotropic dielectric response in myosin, altering the electrostatic potential in the distant actin-binding region and accordingly retracting a positively charged actin-binding loop. A large-scale rearrangement of electrostatic bond network was found to occur upon ATP binding. Since proteins are dielectric and ligands are charged/polar in general, the dielectric allostery might underlie a wide spectrum of functions by proteins.

本文言語English
ページ(範囲)13047-13055
ページ数9
ジャーナルJournal of Physical Chemistry B
120
51
DOI
出版ステータスPublished - 2016 12 29

ASJC Scopus subject areas

  • 物理化学および理論化学
  • 表面、皮膜および薄膜
  • 材料化学

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