PDBsum entry 1sh5

Structural protein

PDB id: 1sh5

Contents

Protein chains

232 a.a. *

Waters ×564

* Residue conservation analysis

PDB id:

1sh5

Name:

Structural protein

Title:

Crystal structure of actin-binding domain of mouse plectin

Structure:

Plectin 1. Chain: a, b. Fragment: actin-binding domain. Synonym: pltn. Pcn. Plectin isoform plec 1,2alpha. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.00Å R-factor: 0.153 R-free: 0.194

Authors:

J.Sevcik,L.Urbanikova

Key ref:

J.Sevcík et al. (2004). Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. Eur J Biochem, 271, 1873-1884. PubMed id: 15128297 DOI: 10.1111/j.1432-1033.2004.04095.x

Date:

25-Feb-04 Release date: 25-May-04

Protein chains

Q9QXS1  (PLEC_MOUSE) -  Plectin from Mus musculus

Seq: 4691 a.a.

Struc: 232 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1111/j.1432-1033.2004.04095.x

Eur J Biochem 271:1873-1884 (2004)

PubMed id: 15128297

Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin.

J.Sevcík, L.Urbániková, J.Kost'an, L.Janda, G.Wiche.

ABSTRACT

Plectin, a large and widely expressed cytolinker protein, is composed of several subdomains that harbor binding sites for a variety of different interaction partners. A canonical actin-binding domain (ABD) comprising two calponin homology domains (CH1 and CH2) is located in proximity to its amino terminus. However, the ABD of plectin is unique among actin-binding proteins as it is expressed in the form of distinct, plectin isoform-specific versions. We have determined the three-dimensional structure of two distinct crystalline forms of one of its ABD versions (pleABD/2alpha) from mouse, to a resolution of 1.95 and 2.0 A. Comparison of pleABD/2alpha with the ABDs of fimbrin and utrophin revealed structural similarity between plectin and fimbrin, although the proteins share only low sequence identity. In fact, pleABD/2alpha has been found to have the same compact fold as the human plectin ABD and the fimbrin ABD, differing from the open conformation described for the ABDs of utrophin and dystrophin. Plectin harbors a specific binding site for intermediate filaments of various types within its carboxy-terminal R5 repeat domain. Our experiments revealed an additional vimentin-binding site of plectin, residing within the CH1 subdomain of its ABD. We show that vimentin binds to this site via the amino-terminal part of its rod domain. This additional amino-terminal intermediate filament protein binding site of plectin may have a function in intermediate filament dynamics and assembly, rather than in linking and stabilizing intermediate filament networks.

Selected figure(s)

Figure 2.
Fig. 2. Ribbon representation of the pleABD/2 structure I and comparison with utrophin and fimbrin ABDs.(A) Stereo view of pleABD/2 . Individual helices are numbered. (B) Crystallographic dimer as seen in the asymmetric unit. The views are related by 90° rotation around a horizontal axis. Molecules A and B are shown in red and blue, respectively. (C) Overlap (stereo view) of CH1 and CH2 subdomains of pleABD/2 molecule A with the CH1 subdomain of utrophin molecule A and the CH2 subdomain of utrophin molecule B. Utrophin molecules are colored in light (molecule A) and dark blue (molecule B). The plectin molecule is in red. (D) Overlap (stereo view) of pleABD/2 (red) with fimbrin ABD (green). Figures were generated using the program MOLSCRIPT[52].

Figure 5.
Fig. 5. Overlay of recombinant vimentin fragments with plectin ABD. Recombinant versions of vimentin subdomains were immobilized on nitrocellulose membranes as described in Fig. 4, and overlaid with the ple1cABD/2 . Vim, full-length vimentin; VimN, N-terminal domain; VimR, rod domain; VimRC, vimentin without N-terminal domain; VimNR, vimentin without C-terminal domain. To detect vimentin-bound plectin ABD, plectin isoform 1c-specific antibodies [31] were used. Note the strong binding of plectin ABD to full-length vimentin and VimNR, but only weak or no binding to other vimentin fragments.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2004, 271, 1873-1884) copyright 2004.

Figures were selected by an automated process.