8OF8

Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)

8OF8 の概要

• エントリーDOI: 10.2210/pdb8of8/pdb
• EMDBエントリー: 16850
• 分子名称: Calmodulin-1, Actin, alpha skeletal muscle, Unconventional myosin-Va (3 entities in total)
• 機能のキーワード: myosin, cytoskeletal motor, myosin-va, myo5a, myosin-5a, s1, rigor, nucleotide free, apo, lever, 6iq, actomyosin, actomyosin-5a, actin, actomyosin-va, actin bound, motor protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 332551.19

構造登録者

Gravett, M.S.C.,Klebl, D.P.,Harlen, O.G.,Read, D.J.,Harris, S.A.,Muench, S.P.,Peckham, M. (登録日: 2023-03-14, 公開日: 2024-09-25, 最終更新日: 2025-04-09)

主引用文献

Gravett, M.S.C.,Klebl, D.P.,Harlen, O.G.,Read, D.J.,Muench, S.P.,Harris, S.A.,Peckham, M.
Exploiting cryo-EM structures of actomyosin-5a to reveal the physical properties of its lever.
Structure, 32:2316-2324.e6, 2024

PubMed Abstract: Myosin 5a (Myo5a) is a dimeric processive motor protein that transports cellular cargos along filamentous actin (F-actin). Its long lever is responsible for its large power-stroke, step size, and load-bearing ability. Little is known about the levers' structure and physical properties, and how they contribute to walking mechanics. Using cryoelectron microscopy (cryo-EM) and molecular dynamics (MD) simulations, we resolved the structure of monomeric Myo5a, comprising the motor domain and full-length lever, bound to F-actin. The range of its lever conformations revealed its physical properties, how stiffness varies along its length and predicts a large, 35 nm, working stroke. Thus, the newly released trail head in a dimeric Myo5a would only need to perform a small diffusive search for its new binding site on F-actin, and stress would only be generated across the dimer once phosphate is released from the lead head, revealing new insight into the walking behavior of Myo5a.

PubMed: 39454567
DOI: 10.1016/j.str.2024.09.025

実験手法

ELECTRON MICROSCOPY (7.5 Å)