PDBsum entry 2x0c

Cell adhesion

PDB id: 2x0c

Contents

Protein chain

308 a.a. *

Waters ×185

* Residue conservation analysis

PDB id:

2x0c

Name:

Cell adhesion

Title:

Crystal structure of the r7r8 domains of talin

Structure:

Talin-1. Chain: a. Fragment: residues 1359-1659. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Variant: talin1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.00Å R-factor: 0.214 R-free: 0.264

Authors:

A.R.Gingras,B.T.Goult,N.Bate,I.L.Barsukov,J.Emsley,D.R.Critchely

Key ref:

A.R.Gingras et al. (2010). Central region of talin has a unique fold that binds vinculin and actin. J Biol Chem, 285, 29577-29587. PubMed id: 20610383

Date:

08-Dec-09 Release date: 07-Jul-10

Protein chain

P26039  (TLN1_MOUSE) -  Talin-1 from Mus musculus

Seq: 2541 a.a.

Struc: 308 a.a.*

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

J Biol Chem 285:29577-29587 (2010)

PubMed id: 20610383

Central region of talin has a unique fold that binds vinculin and actin.

A.R.Gingras, N.Bate, B.T.Goult, B.Patel, P.M.Kopp, J.Emsley, I.L.Barsukov, G.C.Roberts, D.R.Critchley.

ABSTRACT

Talin is an adaptor protein that couples integrins to F-actin. Structural studies show that the N-terminal talin head contains an atypical FERM domain while the N- and C-terminal parts of the talin rod comprise a series of alpha-helical bundles. However, determining the structure of the central part of the rod has proved problematic. Residues 1359-1659 are homologous to the MESDc1 gene product, and we therefore expressed this region of talin in E. coli. The crystal structure shows a unique fold comprised of a 5- and 4-helix bundle. The 5-helix bundle is composed of non-sequential helices due to insertion of the 4-helix bundle into the loop at the C-terminus of helix alpha3. The linker connecting the bundles forms a two-stranded anti-parallel beta-sheet likely limiting the relative movement of the two bundles. Because the 5-helix bundle contains the N- and C-termini of this module, we propose that it is linked by short loops to adjacent bundles while the 4-helix bundle protrudes from the rod. This suggests the 4-helix bundle has a unique role, and its pI (7.8) is higher than other rod domains. Both helical bundles contain vinculin-binding sites, but that in the isolated 5-helix bundle is cryptic whereas that in the isolated 4-helix bundle is constitutively active. In contrast, both bundles are required for actin binding. Finally, we show that the MESDc1 protein, which is predicted to have a similar fold, is a novel actin binding protein.