Long-range coupling between ATP-binding and lever-arm regions in myosin via dielectric allostery

Takato Sato, Jun Ohnuki, Mitsunori Takano*

*この研究の対応する著者

研究成果: Article査読

7 被引用数 (Scopus)

抄録

A protein molecule is a dielectric substance, so the binding of a ligand is expected to induce dielectric response in the protein molecule, considering that ligands are charged or polar in general. We previously reported that binding of adenosine triphosphate (ATP) to molecular motor myosin actually induces such a dielectric response in myosin due to the net negative charge of ATP. By this dielectric response, referred to as "dielectric allostery," spatially separated two regions in myosin, the ATP-binding region and the actin-binding region, are allosterically coupled. In this study, from the statistically stringent analyses of the extensive molecular dynamics simulation data obtained in the ATP-free and the ATP-bound states, we show that there exists the dielectric allostery that transmits the signal of ATP binding toward the distant lever-arm region. The ATP-binding-induced electrostatic potential change observed on the surface of the main domain induced a movement of the converter subdomain from which the lever arm extends. The dielectric response was found to be caused by an underlying large-scale concerted rearrangement of the electrostatic bond network, in which highly conserved charged/polar residues are involved. Our study suggests the importance of the dielectric property for molecular machines in exerting their function.

本文言語English
論文番号215101
ジャーナルJournal of Chemical Physics
147
21
DOI
出版ステータスPublished - 2017 12 7

ASJC Scopus subject areas

  • 物理学および天文学(全般)
  • 物理化学および理論化学

フィンガープリント

「Long-range coupling between ATP-binding and lever-arm regions in myosin via dielectric allostery」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル