3BQ3
Crystal structure of S. cerevisiae Dcn1
Summary for 3BQ3
| Entry DOI | 10.2210/pdb3bq3/pdb |
| Descriptor | Defective in cullin neddylation protein 1, GLYCEROL (3 entities in total) |
| Functional Keywords | ubiquitin, nedd8, neddylation, ubiquitination, scf, cullin, e3 ligases, e2, cell cycle, protein degradation, ligase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 32589.18 |
| Authors | Chou, Y.C.,Sicheri, F. (deposition date: 2007-12-19, release date: 2008-01-29, Last modification date: 2024-11-20) |
| Primary citation | Kurz, T.,Chou, Y.C.,Willems, A.R.,Meyer-Schaller, N.,Hecht, M.L.,Tyers, M.,Peter, M.,Sicheri, F. Dcn1 Functions as a Scaffold-Type E3 Ligase for Cullin Neddylation. Mol.Cell, 29:23-35, 2008 Cited by PubMed Abstract: Cullin-based E3 ubiquitin ligases are activated through modification of the cullin subunit with the ubiquitin-like protein Nedd8. Dcn1 regulates cullin neddylation and thus ubiquitin ligase activity. Here we describe the 1.9 A X-ray crystal structure of yeast Dcn1 encompassing an N-terminal ubiquitin-binding (UBA) domain and a C-terminal domain of unique architecture, which we termed PONY domain. A conserved surface on Dcn1 is required for direct binding to cullins and for neddylation. The reciprocal binding site for Dcn1 on Cdc53 is located approximately 18 A from the site of neddylation. Dcn1 does not require cysteine residues for catalytic function, and directly interacts with the Nedd8 E2 Ubc12 on a surface that overlaps with the E1-binding site. We show that Dcn1 is necessary and sufficient for cullin neddylation in a purified recombinant system. Taken together, these data demonstrate that Dcn1 is a scaffold-like E3 ligase for cullin neddylation. PubMed: 18206966DOI: 10.1016/j.molcel.2007.12.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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