1PEV

Crystal Structure of the Actin Interacting Protein from Caenorhabditis Elegans

Summary for 1PEV

• Entry DOI: 10.2210/pdb1pev/pdb
• Related: 1NR0
• Descriptor: Actin interacting protein 1 (2 entities in total)
• Functional Keywords: beta propeller, wd40 repeat, actin interacting protein, adf, cofilin, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, structural protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 65392.88

Authors

Vorobiev, S.,Mohri, K.,Fedorov, A.A.,Ono, S.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-05-22, release date: 2003-07-01, Last modification date: 2023-08-16)

Primary citation

Mohri, K.,Vorobiev, S.,Fedorov, A.A.,Almo, S.C.,Ono, S.
Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments.
J.Biol.Chem., 279:31697-31707, 2004

PubMed Abstract: 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.

PubMed: 15150269
DOI: 10.1074/jbc.M403351200

Experimental method

X-RAY DIFFRACTION (2 Å)