5CJ1

Crystal structure of the coiled coil of MYH7 residues 1526 to 1571 fused to Gp7

5CJ1 の概要

• エントリーDOI: 10.2210/pdb5cj1/pdb
• 関連するPDBエントリー: 5CHX 5CJ0 5CJ4
• 分子名称: Gp7-MYH7-(1526-1571) chimera protein (2 entities in total)
• 機能のキーワード: motor protein, myosin, coiled coil, fusion
• 由来する生物種: Bacillus phage phi29; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 92382.38

構造登録者

Taylor, K.C.,Korkmaz, E.N.,Andreas, M.P.,Ajay, G.,Heinz, N.T.,Cui, Q.,Rayment, I. (登録日: 2015-07-13, 公開日: 2015-12-02, 最終更新日: 2023-09-27)

主引用文献

Korkmaz, E.N.,Taylor, K.C.,Andreas, M.P.,Ajay, G.,Heinze, N.T.,Cui, Q.,Rayment, I.
A composite approach towards a complete model of the myosin rod.
Proteins, 84:172-189, 2016

PubMed Abstract: Sarcomeric myosins have the remarkable ability to form regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. This has been established for over 50 years and yet a molecular model for the thick filament has not been attained. In part this is due to the lack of a detailed molecular model for the coiled-coil that constitutes the myosin rod. The ability to self-assemble resides in the C-terminal section of myosin known as light meromyosin (LMM) which exhibits strong salt-dependent aggregation that has inhibited structural studies. Here we evaluate the feasibility of generating a complete model for the myosin rod by combining overlapping structures of five sections of coiled-coil covering 164 amino acid residues which constitute 20% of LMM. Each section contains ∼ 7-9 heptads of myosin. The problem of aggregation was overcome by incorporating the globular folding domains, Gp7 and Xrcc4 which enhance crystallization. The effect of these domains on the stability and conformation of the myosin rod was examined through biophysical studies and overlapping structures. In addition, a computational approach was developed to combine the sections into a contiguous model. The structures were aligned, trimmed to form a contiguous model, and simulated for >700 ns to remove the discontinuities and achieve an equilibrated conformation that represents the native state. This experimental and computational strategy lays the foundation for building a model for the entire myosin rod.

PubMed: 26573747
DOI: 10.1002/prot.24964

実験手法

X-RAY DIFFRACTION (2.1 Å)