6T1Y

Cryo-EM structure of phalloidin-stabilized F-actin (copolymerized)

6T1Y の概要

• エントリーDOI: 10.2210/pdb6t1y/pdb
• 関連するPDBエントリー: 5OOC 5OOD 6T20 6T23 6T24 6T25
• EMDBエントリー: 10363 10364 10365 10366 10367 3836 3837
• 分子名称: Actin, alpha skeletal muscle, phalloidin, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: cytoskeleton, phalloidin, stabilized-actin filament, structural protein
• 由来する生物種: Oryctolagus cuniculus (Rabbit); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 215680.19

構造登録者

Pospich, S.,Merino, F.,Raunser, S. (登録日: 2019-10-07, 公開日: 2020-03-04, 最終更新日: 2025-04-09)

主引用文献

Pospich, S.,Merino, F.,Raunser, S.
Structural Effects and Functional Implications of Phalloidin and Jasplakinolide Binding to Actin Filaments.
Structure, 28:437-449.e5, 2020

PubMed Abstract: Actin undergoes structural transitions during polymerization, ATP hydrolysis, and subsequent release of inorganic phosphate. Several actin-binding proteins sense specific states during this transition and can thus target different regions of the actin filament. Here, we show in atomic detail that phalloidin, a mushroom toxin that is routinely used to stabilize and label actin filaments, suspends the structural changes in actin, likely influencing its interaction with actin-binding proteins. Furthermore, high-resolution cryoelectron microscopy structures reveal structural rearrangements in F-actin upon inorganic phosphate release in phalloidin-stabilized filaments. We find that the effect of the sponge toxin jasplakinolide differs from the one of phalloidin, despite their overlapping binding site and similar interactions with the actin filament. Analysis of structural conformations of F-actin suggests that stabilizing agents trap states within the natural conformational space of actin.

PubMed: 32084355
DOI: 10.1016/j.str.2020.01.014

実験手法

ELECTRON MICROSCOPY (3.3 Å)