PDBsum entry 2aq5

Structural protein

PDB id: 2aq5

Contents

Protein chain

395 a.a. *

Waters ×463

* Residue conservation analysis

PDB id:

2aq5

Name:

Structural protein

Title:

Crystal structure of murine coronin-1

Structure:

Coronin-1a. Chain: a. Synonym: coronin-like protein p57, coronin-like protein a, clipina, tryptophan aspartate-containing coat protein, taco. Engineered: yes

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Gene: coro1a, coro1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108

Resolution:

1.75Å R-factor: 0.160 R-free: 0.192

Authors:

B.A.Appleton,P.Wu,C.Wiesmann

Key ref:

B.A.Appleton et al. (2006). The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes. Structure, 14, 87-96. PubMed id: 16407068 DOI: 10.1016/j.str.2005.09.013

Date:

17-Aug-05 Release date: 06-Dec-05

Protein chain

O89053  (COR1A_MOUSE) -  Coronin-1A from Mus musculus

Seq: 461 a.a.

Struc: 395 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

DOI no: 10.1016/j.str.2005.09.013

Structure 14:87-96 (2006)

PubMed id: 16407068

The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes.

B.A.Appleton, P.Wu, C.Wiesmann.

ABSTRACT

Mammalian coronin-1 is preferentially expressed in hematopoietic cells and plays a poorly understood role in the dynamic reorganization of the actin cytoskeleton. Sequence analysis of coronin-1 revealed five WD40 repeats that were predicted to form a beta propeller. They are followed by a 130 residue extension and a 30 residue leucine zipper domain that is responsible for multimerization of the protein. Here, we present the crystal structure of murine coronin-1 without the leucine zipper at 1.75 A resolution. Coronin-1 forms a seven-bladed beta propeller composed of the five predicted WD40 repeats and two additional blades that lack any homology to the canonical WD40 motif. The C-terminal extension adopts an extended conformation, packs tightly against the bottom surface of the propeller, and is likely to be required for the structural stability of the propeller. Analysis of charged and conserved surface residues delineate possible binding sites for F-actin on the beta propeller.

Selected figure(s)

Figure 1.
Figure 1. The Overall Structure of Murine Coronin-1
(A) Ribbon diagrams of coronin-1 showing the "top" (left) and "bottom" (right) side of the b propeller. The structure can be divided into an N-terminal seven-bladed b propeller (residues 8-352; colored blue, yellow, and green) and a C-terminal extension (residues 353-402; colored red). The last ordered residues of the N and C termini are marked with an "NT" and "CT," respectively. The individual blades are numbered from one to seven; the strands in each blade are named A-D and are labeled in blade 4.
(B) The "side" view highlights the C-terminal extension (red) tightly packing against the "bottom" surface of the propeller. The structure lacks the C-terminal leucine zipper responsible for multimerization (Gatfield et al., 2005 and Oku et al., 2005), and, accordingly, the protein is monomeric. All figures were generated with PyMol (DeLano, 2002).

The above figure is reprinted by permission from Cell Press: Structure (2006, 14, 87-96) copyright 2006.

Figure was selected by an automated process.