PDBsum entry: 1wm4

Protein binding

PDB id: 1wm4

Contents

Protein chain

142 a.a. *

* Residue conservation analysis

PDB id:

1wm4

Name:

Protein binding

Title:

Solution structure of mouse coactosin, an actin filament binding protein

Structure:

Coactosin-like protein. Chain: a. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

15 models

Authors:

M.Hellman,V.O.Paavilainen,P.Naumanen,P.Lappalainen,A.Annila, P.Permi

Key ref:

M.Hellman et al. (2004). Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins. FEBS Lett, 576, 91-96. PubMed id: 15474017 DOI: 10.1016/j.febslet.2004.08.068

Date:

03-Jul-04 Release date: 02-Nov-04

Protein chain

Q9CQI6  (COTL1_MOUSE) -  Coactosin-like protein

Seq: 142 a.a.

Struc: 142 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cellular_component (4 terms)
• Biological process: defense response to fungus (1 term)
• Biochemical function: protein binding (3 terms)

DOI no: 10.1016/j.febslet.2004.08.068

FEBS Lett 576:91-96 (2004)

PubMed id: 15474017

Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins.

M.Hellman, V.O.Paavilainen, P.Naumanen, P.Lappalainen, A.Annila, P.Permi.

ABSTRACT

Coactosin is a small (MW approximately 15 kDa) evolutionarily conserved actin filament binding protein. It displays remote sequence homology to ADF/cofilin proteins and to the ADF-H domains of twinfilin and Abp1/drebrin. However, biochemical analyses have demonstrated that coactosin has a very different role in actin dynamics from the ones of ADF/cofilin, twinfilin or Abp1/drebrin. To elucidate the molecular mechanism of coactosin/actin interaction, we determined the three-dimensional structure of mouse coactosin by multidimensional NMR spectroscopy. We find that the coactosin structure is homologous to ADF/cofilin and to the ADF-H domains of twinfilin. Furthermore, the regions that have been shown to be important for actin filament interactions in ADF/cofilins are structurally conserved in coactosin suggesting that these two proteins interact with F-actin through a conserved interface. Our analysis also identifies key structural differences between these proteins that may account for the differences in biochemical activities and cellular roles of these proteins.

Selected figure(s)

Figure 1.
Fig. 1. Overall structure of the coactosin protein. (A) Main chain representation of the (15) lowest energy structures superimposed on one another. Residues are color-coded according to the T[2] relaxation times. Dark blue represents the residues with T[2] close to the mean value (region indicated with residue numbers), violet when 35–90% and magenta when over 90% increase in T[2]‘s were observed and light blue when not measured. (B) A schematic ribbon representation of coactosin. The structure is colored from green (N-terminus) via blue to red to orange (C-terminus). (C) Same as (B) after a 120° rotation relative to the vertical axis. This and all subsequent figures were produced with the program MOLMOL [33] unless otherwise stated.

Figure 3.
Fig. 3. Representation of the structural basis of the stabilization of the long α3-helix (A) in coactosin and (C) in yeast cofilin (highly conserved in the ADF-H domains). In (B) and (D) are shown the same models as in A and C, respectively, rotated by 90° relative to y-axis. Locations of the important residues in the primary structure are shown in Fig. 2A with circles and are colored according to their position. Corresponding secondary structure elements are marked with similar but lighter shading.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2004, 576, 91-96) copyright 2004.

Figures were selected by the author.