1pev

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spinqualitylabelsall models 1pev, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans

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

1PEV 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

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