5I4E

Crystal Structure of Human Nonmuscle Myosin 2C motor domain

「2YCU」から置き換えられました

5I4E の概要

• エントリーDOI: 10.2210/pdb5i4e/pdb
• 分子名称: Myosin-14,Alpha-actinin A, ADP ORTHOVANADATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: motor protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 112157.25

構造登録者

Chinthalapudi, K.,Heissler, S.M.,Preller, M.,Sellers, J.R.,Manstein, D.J. (登録日: 2016-02-11, 公開日: 2017-09-13, 最終更新日: 2024-01-10)

主引用文献

Chinthalapudi, K.,Heissler, S.M.,Preller, M.,Sellers, J.R.,Manstein, D.J.
Mechanistic insights into the active site and allosteric communication pathways in human nonmuscle myosin-2C.
Elife, 6:-, 2017

PubMed Abstract: Despite a generic, highly conserved motor domain, ATP turnover kinetics and their activation by F-actin vary greatly between myosin-2 isoforms. Here, we present a 2.25 Å pre-powerstroke state (ADP⋅VO) crystal structure of the human nonmuscle myosin-2C motor domain, one of the slowest myosins characterized. In combination with integrated mutagenesis, ensemble-solution kinetics, and molecular dynamics simulation approaches, the structure reveals an allosteric communication pathway that connects the distal end of the motor domain with the active site. Disruption of this pathway by mutation of hub residue R788, which forms the center of a cluster of interactions connecting the converter, the SH1-SH2 helix, the relay helix, and the lever, abolishes nonmuscle myosin-2 specific kinetic signatures. Our results provide insights into structural changes in the myosin motor domain that are triggered upon F-actin binding and contribute critically to the mechanochemical behavior of stress fibers, actin arcs, and cortical actin-based structures.

PubMed: 29256864
DOI: 10.7554/eLife.32742

実験手法

X-RAY DIFFRACTION (2.25 Å)