2OS8

Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor

2OS8 の概要

• エントリーDOI: 10.2210/pdb2os8/pdb
• 関連するPDBエントリー: 1kk7 1kk8 1OE9 1sr6
• 分子名称: Myosin heavy chain, Myosin regulatory light chain, Myosin essential light chain, ... (5 entities in total)
• 機能のキーワード: myosin s1, rigor-like, motor, mechanical elements, contractile protein
• 由来する生物種: Placopecten magellanicus (sea scallop); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 131784.62

構造登録者

Yang, Y.,Gourinath, S.,Cohen, C.,Brown, J.H. (登録日: 2007-02-05, 公開日: 2007-05-29, 最終更新日: 2023-08-30)

主引用文献

Yang, Y.,Gourinath, S.,Kovacs, M.,Nyitray, L.,Reutzel, R.,Himmel, D.M.,O'neall-Hennessey, E.,Reshetnikova, L.,Szent-Gyorgyi, A.G.,Brown, J.H.,Cohen, C.
Rigor-like Structures from Muscle Myosins Reveal Key Mechanical Elements in the Transduction Pathways of This Allosteric Motor.
Structure, 15:553-564, 2007

PubMed Abstract: Unlike processive cellular motors such as myosin V, whose structure has recently been determined in a "rigor-like" conformation, myosin II from contracting muscle filaments necessarily spends most of its time detached from actin. By using squid and sea scallop sources, however, we have now obtained similar rigor-like atomic structures for muscle myosin heads (S1). The significance of the hallmark closed actin-binding cleft in these crystal structures is supported here by actin/S1-binding studies. These structures reveal how different duty ratios, and hence cellular functions, of the myosin isoforms may be accounted for, in part, on the basis of detailed differences in interdomain contacts. Moreover, the rigor-like position of switch II turns out to be unique for myosin V. The overall arrangements of subdomains in the motor are relatively conserved in each of the known contractile states, and we explore qualitatively the energetics of these states.

PubMed: 17502101
DOI: 10.1016/j.str.2007.03.010

実験手法

X-RAY DIFFRACTION (3.27 Å)