期刊
DEVELOPMENTAL CELL
卷 33, 期 4, 页码 401-412出版社
CELL PRESS
DOI: 10.1016/j.devcel.2015.03.025
关键词
-
资金
- CNRS
- Equipes FRM
- ANR [2010 BLAN 1504 01, ANR-13-BSV8-0019-01]
- Ligue Contre le Cancer
- ARC subvention fixe
- NIH [DC009100, HL110869]
- Agence Nationale de la Recherche (ANR) [ANR-13-BSV8-0019] Funding Source: Agence Nationale de la Recherche (ANR)
Fundamental to cellular processes are directional movements driven by molecular motors. A common theme for these and other molecular machines driven by ATP is that controlled release of hydrolysis products is essential for using the chemical energy efficiently. Mechanochemical transduction by myosin motors on actin is coupled to unknown structural changes that result in the sequential release of inorganic phosphate (P-i) and MgADP. We present here a myosin structure possessing an actin-binding interface and a tunnel (back door) that creates an escape route for P-i with a minimal rotation of the myosin lever arm that drives movements. We propose that this state represents the beginning of the powerstroke on actin and that P-i translocation from the nucleotide pocket triggered by actin binding initiates myosin force generation. This elucidates how actin initiates force generation and movement and may represent a strategy common to many molecular machines.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据