4E7S

Myosin VI D23R I24R R569E (MD) pre-powerstroke state

4E7S の概要

• エントリーDOI: 10.2210/pdb4e7s/pdb
• 関連するPDBエントリー: 4E7Z
• 分子名称: Myosin-VI, ADENOSINE-5'-DIPHOSPHATE, VANADATE ION, ... (7 entities in total)
• 機能のキーワード: myosin, molecular motor, motor protein
• 由来する生物種: Sus scrofa (pigs,swine,wild boar)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 183961.35

構造登録者

Isabet, T.,Sweeney, H.L.,Houdusse, A. (登録日: 2012-03-19, 公開日: 2012-09-19, 最終更新日: 2024-02-28)

主引用文献

Menetrey, J.,Isabet, T.,Ropars, V.,Mukherjea, M.,Pylypenko, O.,Liu, X.,Perez, J.,Vachette, P.,Sweeney, H.L.,Houdusse, A.M.
Processive Steps in the Reverse Direction Require Uncoupling of the Lead Head Lever Arm of Myosin VI.
Mol.Cell, 48:75-86, 2012

PubMed Abstract: Myosin VI is the only known reverse-direction myosin motor. It has an unprecedented means of amplifying movements within the motor involving rearrangements of the converter subdomain at the C terminus of the motor and an unusual lever arm projecting from the converter. While the average step size of a myosin VI dimer is 30-36 nm, the step size is highly variable, presenting a challenge to the lever arm mechanism by which all myosins are thought to move. Herein, we present structures of myosin VI that reveal regions of compliance that allow an uncoupling of the lead head when movement is modeled on actin. The location of the compliance restricts the possible actin binding sites and predicts the observed stepping behavior. The model reveals that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model.

PubMed: 22940248
DOI: 10.1016/j.molcel.2012.07.034

実験手法

X-RAY DIFFRACTION (2.25 Å)