1pev

File:1pev.gif

spinqualitylabelsall models PDB ID 1pev Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.00Å
Gene:	UNC-78 OR C04F6.4 (Caenorhabditis elegans)
Coordinates:	save as pdb, mmCIF, xml

Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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