5OOD

Cryo-EM structure of jasplakinolide-stabilized F-actin in complex with ADP-Pi

5OOD の概要

• エントリーDOI: 10.2210/pdb5ood/pdb
• 関連するPDBエントリー: 5ONV 5OOC 5OOE 5OOF 6T1Y 6T20 6T23 6T24 6T25
• EMDBエントリー: 10363 10364 10365 10366 10367 3835 3836 3837 3838 3839
• 分子名称: Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: cytoskeleton, nucleotide states, filament stability, cell migration, structural protein
• 由来する生物種: Oryctolagus cuniculus (Rabbit)
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 215479.76

構造登録者

Merino, F.,Pospich, S.,Funk, J.,Kuellmer, F.,Arndt, H.-D.,Bieling, P.,Raunser, S. (登録日: 2017-08-07, 公開日: 2018-06-13, 最終更新日: 2025-04-09)

主引用文献

Merino, F.,Pospich, S.,Funk, J.,Wagner, T.,Kullmer, F.,Arndt, H.D.,Bieling, P.,Raunser, S.
Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.
Nat. Struct. Mol. Biol., 25:528-537, 2018

PubMed Abstract: The function of actin is coupled to the nucleotide bound to its active site. ATP hydrolysis is activated during polymerization; a delay between hydrolysis and inorganic phosphate (P) release results in a gradient of ATP, ADP-P and ADP along actin filaments (F-actin). Actin-binding proteins can recognize F-actin's nucleotide state, using it as a local 'age' tag. The underlying mechanism is complex and poorly understood. Here we report six high-resolution cryo-EM structures of F-actin from rabbit skeletal muscle in different nucleotide states. The structures reveal that actin polymerization repositions the proposed catalytic base, His161, closer to the γ-phosphate. Nucleotide hydrolysis and P release modulate the conformational ensemble at the periphery of the filament, thus resulting in open and closed states, which can be sensed by coronin-1B. The drug-like toxin jasplakinolide locks F-actin in an open state. Our results demonstrate in detail how ATP hydrolysis links to F-actin's conformational dynamics and protein interaction.

PubMed: 29867215
DOI: 10.1038/s41594-018-0074-0

実験手法

ELECTRON MICROSCOPY (3.7 Å)