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1nr0

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Revision as of 11:00, 20 March 2008 by OCA (Talk | contribs)
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Image:1nr0.gif


PDB ID 1nr0

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Gene: UNC-78 OR C04F6.4 (Caenorhabditis elegans)
Coordinates: save as pdb, mmCIF, xml



Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).


Overview

Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping.

About this Structure

1NR0 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.

Reference

Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments., Mohri K, Vorobiev S, Fedorov AA, Almo SC, Ono S, J Biol Chem. 2004 Jul 23;279(30):31697-707. Epub 2004 May 18. PMID:15150269

Page seeded by OCA on Thu Mar 20 13:00:32 2008

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