4PFP

Myosin VI motor domain in the Pi release state (with Pi) space group P21

4PFP の概要

• エントリーDOI: 10.2210/pdb4pfp/pdb
• 関連するPDBエントリー: 4PFO
• 分子名称: Unconventional myosin-VI, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: motor protein, pi release state, motor domain
• 由来する生物種: Sus scrofa (Pig)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 180958.38

構造登録者

Isabet, T.,Benisty, H.,Llinas, P.,Sweeney, H.L.,Houdusse, A. (登録日: 2014-04-30, 公開日: 2015-04-29, 最終更新日: 2024-05-08)

主引用文献

Llinas, P.,Isabet, T.,Song, L.,Ropars, V.,Zong, B.,Benisty, H.,Sirigu, S.,Morris, C.,Kikuti, C.,Safer, D.,Sweeney, H.L.,Houdusse, A.
How actin initiates the motor activity of Myosin.
Dev.Cell, 33:401-412, 2015

PubMed Abstract: 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 (Pi) and MgADP. We present here a myosin structure possessing an actin-binding interface and a tunnel (back door) that creates an escape route for Pi 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 Pi 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.

PubMed: 25936506
DOI: 10.1016/j.devcel.2015.03.025

実験手法

X-RAY DIFFRACTION (2.32 Å)