3bq3

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Revision as of 09:04, 31 January 2008

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spinqualitylabelsall models 3bq3, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of S. cerevisiae Dcn1

Overview

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.

About this Structure

3BQ3 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Dcn1 functions as a scaffold-type e3 ligase for cullin neddylation., Kurz T, Chou YC, Willems AR, Meyer-Schaller N, Hecht ML, Tyers M, Peter M, Sicheri F, Mol Cell. 2008 Jan 18;29(1):23-35. PMID:18206966

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