2AQ5

Crystal Structure of Murine Coronin-1

Summary for 2AQ5

• Entry DOI: 10.2210/pdb2aq5/pdb
• Related: 2B4E
• Descriptor: Coronin-1A (2 entities in total)
• Functional Keywords: wd40 repeat, 7-bladed beta-propeller, structural protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm, cytoskeleton: O89053
• Total number of polymer chains: 1
• Total formula weight: 44500.80

Authors

Appleton, B.A.,Wu, P.,Wiesmann, C. (deposition date: 2005-08-17, release date: 2005-12-06, Last modification date: 2024-10-30)

Primary citation

Appleton, B.A.,Wu, P.,Wiesmann, C.
The crystal structure of murine coronin-1: a regulator of actin cytoskeletal dynamics in lymphocytes.
Structure, 14:87-96, 2006

PubMed 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.

PubMed: 16407068
DOI: 10.1016/j.str.2005.09.013

Experimental method

X-RAY DIFFRACTION (1.75 Å)