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Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation.
Journal article

Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation.

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  • 2008-01-22
Published in:
  • Molecular cell. - 2008
Amino Acid Sequence
Binding Sites
Catalysis
Conserved Sequence
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Interaction Mapping
Protein Processing, Post-Translational
Protein Structure, Tertiary
Recombinant Fusion Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Ubiquitin
Ubiquitin-Protein Ligases
Ubiquitination
Ubiquitins
English 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.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.rero.ch/global/documents/233972
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