1NR0
Two Seven-Bladed Beta-Propeller Domains Revealed By The Structure Of A C. elegans Homologue Of Yeast Actin Interacting Protein 1 (AIP1).
Summary for 1NR0
| Entry DOI | 10.2210/pdb1nr0/pdb |
| Descriptor | Actin interacting protein 1, MANGANESE (II) ION (3 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 | 65447.82 |
| Authors | Vorobiev, S.M.,Mohri, K.,Ono, S.,Almo, S.C.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-01-23, release date: 2003-07-01, Last modification date: 2024-02-14) |
| Primary citation | Mohri, K.,Vorobiev, S.M.,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 Cited by 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: 15150269DOI: 10.1074/jbc.M403351200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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