PDBsum entry: 1t2l

Protein binding

PDB id: 1t2l

Contents

Protein chains

136 a.a. *

Waters ×27

* Residue conservation analysis

PDB id:

1t2l

Name:

Protein binding

Title:

Three crystal structures of human coactosin-like protein

Structure:

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

Source:

Homo sapiens. Human. Organism_taxid: 9606. Strain: b834(de3). Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.80Å R-factor: 0.197 R-free: 0.269

Authors:

L.Liu,Z.Wei,Z.Chen,Y.Wang,W.Gong

Key ref:

L.Liu et al. (2004). Crystal structure of human coactosin-like protein. J Mol Biol, 344, 317-323. PubMed id: 15522287 DOI: 10.1016/j.jmb.2004.09.036

Date:

22-Apr-04 Release date: 23-Nov-04

Protein chains

Q14019  (COTL1_HUMAN) -  Coactosin-like protein

Seq: 142 a.a.

Struc: 136 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cellular_component (4 terms)
• Biological process: biological_process (2 terms)
• Biochemical function: protein binding (3 terms)

DOI no: 10.1016/j.jmb.2004.09.036

J Mol Biol 344:317-323 (2004)

PubMed id: 15522287

Crystal structure of human coactosin-like protein.

L.Liu, Z.Wei, Y.Wang, M.Wan, Z.Cheng, W.Gong.

ABSTRACT

Human coactosin-like protein is an actin filament binding protein but does not bind to globular actin. It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of capping protein which inhibits the actin polymerization. We determined the crystal structures of human coactosin-like protein by multi-wavelength anomalous dispersion method. The structure showed a high level of similarity to ADF-H domain, although their amino acid sequences share low degree of homology. A few conserved hydrophobic residues that may contribute to the folding were identified. This structure suggests coactosin-like protein bind to F-actin in a different way from ADF/Cofilin family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin and 5-Lipoxygenase from binding to coactosin simultaneously.

Selected figure(s)

Figure 1.
Figure 1. The stereo view of ribbon diagram of human CLP. The six-stranded mixed b-sheet is in purple; the helices are in light-green; and the connecting loops are in gray. Structural elements are labeled in the left diagram. Figure 1, Figure 2 and Figure 3 were prepared using Ribbons.17

Figure 2.
Figure 2. The two monomers of human CLP. (A) The ribbons diagram of two human CLP monomers packing in an asymmetric unit. The two monomers are related by a non-crystallographic 2-fold screw axis. (B) The stereo view of the superposition of the two monomers (green and red), NMR structure of human CLP (blue), and NMR structure of mouse CLP (yellow). The structural difference of these four structures, the loop connecting b4 and b5, are shadowed. Actin-binding site Lys75 and 5LO binding site Lys131 are showed in stick and ball model (purple). The each model of the two NMR structures used for superposition is the first model of 20 models. The N termini (residues before initial Met) and the C termini (residues after Ala132) of the selected models are cut before superposition, because the N termini do not exist in nature structure and the N- and C termini are highly disordered in the two NMR structures.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2004, 344, 317-323) copyright 2004.

Figures were selected by an automated process.