PDBsum entry 7dsa

Cytosolic protein

PDB id: 7dsa

Contents

Protein chains

264 a.a.

239 a.a.

117 a.a.

Metals

_MG ×2

Waters ×101

PDB id:

7dsa

Name:

Cytosolic protein

Title:

Crystal structure of actin capping protein in complex with v-1 (space group p62)

Structure:

F-actin-capping protein subunit alpha-1. Chain: a. Synonym: beta-actinin subunit i,capz 36/32. Engineered: yes. F-actin-capping protein subunit beta isoforms 1. Chain: b. Synonym: beta-actinin subunit ii,capz 36/32,capz b1 and b2. Engineered: yes. Myotrophin.

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Gene: capza1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: capzb. Homo sapiens. Human.

Resolution:

2.80Å R-factor: 0.215 R-free: 0.254

Authors:

S.Takeda

Key ref:

S.Takeda et al. (2021). Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail. J Mol Biol, 433, 166891-166891. PubMed id: 33639213 DOI: 10.1016/j.jmb.2021.166891

Date:

30-Dec-20 Release date: 03-Mar-21

Protein chain

P13127  (CAZA1_CHICK) -  F-actin-capping protein subunit alpha-1 from Gallus gallus

Seq: 286 a.a.

Struc: 264 a.a.

Protein chain

P14315  (CAPZB_CHICK) -  F-actin-capping protein subunit beta isoforms 1 and 2 from Gallus gallus

Seq: 277 a.a.

Struc: 239 a.a.

Protein chain

P58546  (MTPN_HUMAN) -  Myotrophin from Homo sapiens

Seq: 118 a.a.

Struc: 117 a.a.

DOI no: 10.1016/j.jmb.2021.166891

J Mol Biol 433:166891-166891 (2021)

PubMed id: 33639213

Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail.

S.Takeda, R.Koike, I.Fujiwara, A.Narita, M.Miyata, M.Ota, Y.Maéda.

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.