6BNU

Structure of bare actin filament, backbone-averaged with sidechains truncated to alanine

6BNU の概要

• エントリーDOI: 10.2210/pdb6bnu/pdb
• 関連するPDBエントリー: 6BNO
• EMDBエントリー: 7115 7116 7117
• 分子名称: Actin, alpha skeletal muscle (1 entity in total)
• 機能のキーワード: cytoskeleton, filament, contractile protein
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• 細胞内の位置: Cytoplasm, cytoskeleton: P68135
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 332482.13

構造登録者

Gurel, P.S.,Alushin, G.A. (登録日: 2017-11-17, 公開日: 2018-01-10, 最終更新日: 2024-03-13)

主引用文献

Gurel, P.S.,Kim, L.Y.,Ruijgrok, P.V.,Omabegho, T.,Bryant, Z.,Alushin, G.M.
Cryo-EM structures reveal specialization at the myosin VI-actin interface and a mechanism of force sensitivity.
Elife, 6:-, 2017

PubMed Abstract: Despite extensive scrutiny of the myosin superfamily, the lack of high-resolution structures of actin-bound states has prevented a complete description of its mechanochemical cycle and limited insight into how sequence and structural diversification of the motor domain gives rise to specialized functional properties. Here we present cryo-EM structures of the unique minus-end directed myosin VI motor domain in rigor (4.6 Å) and Mg-ADP (5.5 Å) states bound to F-actin. Comparison to the myosin IIC-F-actin rigor complex reveals an almost complete lack of conservation of residues at the actin-myosin interface despite preservation of the primary sequence regions composing it, suggesting an evolutionary path for motor specialization. Additionally, analysis of the transition from ADP to rigor provides a structural rationale for force sensitivity in this step of the mechanochemical cycle. Finally, we observe reciprocal rearrangements in actin and myosin accompanying the transition between these states, supporting a role for actin structural plasticity during force generation by myosin VI.

PubMed: 29199952
DOI: 10.7554/eLife.31125

実験手法

ELECTRON MICROSCOPY (7.5 Å)