7DS2

Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail

7DS2 の概要

• エントリーDOI: 10.2210/pdb7ds2/pdb
• 分子名称: F-actin-capping protein subunit alpha-1, F-actin-capping protein subunit beta isoforms 1, Twinfilin-1, ... (4 entities in total)
• 機能のキーワード: actin dynamics, actin capping protein, twinfilin, carmil, v-1, cytosolic protein
• 由来する生物種: Gallus gallus (Chicken); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 64806.82

構造登録者

Takeda, S. (登録日: 2020-12-30, 公開日: 2021-03-03, 最終更新日: 2023-11-29)

主引用文献

Takeda, S.,Koike, R.,Fujiwara, I.,Narita, A.,Miyata, M.,Ota, M.,Maeda, Y.
Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail.
J.Mol.Biol., 433:166891-166891, 2021

PubMed Abstract: Twinfilin is a conserved actin regulator that interacts with actin capping protein (CP) via C terminus residues (TWtail) that exhibits sequence similarity with the CP interaction (CPI) motif of CARMIL. Here we report the crystal structure of TWtail in complex with CP. Our structure showed that although TWtail and CARMIL CPI bind CP to an overlapping surface via their middle regions, they exhibit different CP-binding modes at both termini. Consequently, TWtail and CARMIL CPI restrict the CP in distinct conformations of open and closed forms, respectively. Interestingly, V-1, which targets CP away from the TWtail binding site, also favors the open-form CP. Consistently, TWtail forms a stable ternary complex with CP and V-1, a striking contrast to CARMIL CPI, which rapidly dissociates V-1 from CP. Our results demonstrate that TWtail is a unique CP-binding motif that regulates CP in a manner distinct from CARMIL CPI.

PubMed: 33639213
DOI: 10.1016/j.jmb.2021.166891

実験手法

X-RAY DIFFRACTION (1.95 Å)