7NEP

Homology model of the in situ actomyosin complex from the A-band of mouse psoas muscle sarcomere in the rigor state

7NEP の概要

• エントリーDOI: 10.2210/pdb7nep/pdb
• EMDBエントリー: 12289
• 分子名称: Actin, alpha skeletal muscle, Tropomyosin alpha-1 chain, Myosin-4, ... (5 entities in total)
• 機能のキーワード: muscle proteins, force generation, sarcomere, cytoskeleton, motor protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 825747.62

構造登録者

Wang, Z.,Grange, M.,Wagner, T.,Kho, A.L.,Gautel, M.,Raunser, S. (登録日: 2021-02-04, 公開日: 2021-04-07, 最終更新日: 2024-05-01)

主引用文献

Wang, Z.,Grange, M.,Wagner, T.,Kho, A.L.,Gautel, M.,Raunser, S.
The molecular basis for sarcomere organization in vertebrate skeletal muscle.
Cell, 184:2135-, 2021

PubMed Abstract: Sarcomeres are force-generating and load-bearing devices of muscles. A precise molecular picture of how sarcomeres are built underpins understanding their role in health and disease. Here, we determine the molecular architecture of native vertebrate skeletal sarcomeres by electron cryo-tomography. Our reconstruction reveals molecular details of the three-dimensional organization and interaction of actin and myosin in the A-band, I-band, and Z-disc and demonstrates that α-actinin cross-links antiparallel actin filaments by forming doublets with 6-nm spacing. Structures of myosin, tropomyosin, and actin at ~10 Å further reveal two conformations of the "double-head" myosin, where the flexible orientation of the lever arm and light chains enable myosin not only to interact with the same actin filament, but also to split between two actin filaments. Our results provide unexpected insights into the fundamental organization of vertebrate skeletal muscle and serve as a strong foundation for future investigations of muscle diseases.

PubMed: 33765442
DOI: 10.1016/j.cell.2021.02.047

実験手法

ELECTRON MICROSCOPY (10.2 Å)