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3bq3

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{{STRUCTURE_3bq3| PDB=3bq3 | SCENE= }}
{{STRUCTURE_3bq3| PDB=3bq3 | SCENE= }}
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'''Crystal structure of S. cerevisiae Dcn1'''
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===Crystal structure of S. cerevisiae Dcn1===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_18206966}}
==About this Structure==
==About this Structure==
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[[Category: Ubiquitin]]
[[Category: Ubiquitin]]
[[Category: Ubiquitination,scf,cullin]]
[[Category: Ubiquitination,scf,cullin]]
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Revision as of 23:00, 27 July 2008

Image:3bq3.png

Template:STRUCTURE 3bq3

Crystal structure of S. cerevisiae Dcn1

Template:ABSTRACT PUBMED 18206966

About this Structure

3BQ3 is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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