7DS6

Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (TWN-CDC)

Summary for 7DS6

• Entry DOI: 10.2210/pdb7ds6/pdb
• Descriptor: F-actin-capping protein subunit alpha-1, F-actin-capping protein subunit beta isoforms 1, Twinfilin-1,CD2-associated protein, ... (4 entities in total)
• Functional Keywords: actin dynamics, actin capping protein, twinfilin, carmil, v-1, cytosolic protein
• Biological source: Gallus gallus (Chicken); More
• Total number of polymer chains: 3
• Total formula weight: 63358.26

Authors

Takeda, S. (deposition date: 2020-12-30, release date: 2021-03-03, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.69 Å)