5I0I

Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state

5I0I の概要

• エントリーDOI: 10.2210/pdb5i0i/pdb
• 関連するPDBエントリー: 5hmo 5hmp 5i0h
• 分子名称: Unconventional myosin-X, SULFATE ION, Calmodulin, ... (11 entities in total)
• 機能のキーワード: myosin, motor domain, molecular motor, pre-powerstrocke state, motility, motor protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cytoplasm, cytosol : Q9HD67
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 230629.74

構造登録者

Isabet, T.,Sweeney, H.L.,Houdusse, A. (登録日: 2016-02-04, 公開日: 2016-09-07, 最終更新日: 2024-05-08)

主引用文献

Ropars, V.,Yang, Z.,Isabet, T.,Blanc, F.,Zhou, K.,Lin, T.,Liu, X.,Hissier, P.,Samazan, F.,Amigues, B.,Yang, E.D.,Park, H.,Pylypenko, O.,Cecchini, M.,Sindelar, C.V.,Sweeney, H.L.,Houdusse, A.
The myosin X motor is optimized for movement on actin bundles.
Nat Commun, 7:12456-12456, 2016

PubMed Abstract: Myosin X has features not found in other myosins. Its structure must underlie its unique ability to generate filopodia, which are essential for neuritogenesis, wound healing, cancer metastasis and some pathogenic infections. By determining high-resolution structures of key components of this motor, and characterizing the in vitro behaviour of the native dimer, we identify the features that explain the myosin X dimer behaviour. Single-molecule studies demonstrate that a native myosin X dimer moves on actin bundles with higher velocities and takes larger steps than on single actin filaments. The largest steps on actin bundles are larger than previously reported for artificially dimerized myosin X constructs or any other myosin. Our model and kinetic data explain why these large steps and high velocities can only occur on bundled filaments. Thus, myosin X functions as an antiparallel dimer in cells with a unique geometry optimized for movement on actin bundles.

PubMed: 27580874
DOI: 10.1038/ncomms12456

実験手法

X-RAY DIFFRACTION (3.15 Å)