2IS9

Structure of yeast DCN-1

Summary for 2IS9

• Entry DOI: 10.2210/pdb2is9/pdb
• Descriptor: Defective in cullin neddylation protein 1, PLATINUM (II) ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: ubiquitin, dcn1, transcription
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 25145.10

Authors

Yang, X.,Zhou, J.,Sun, L.,Wei, Z.,Gao, J.,Gong, W.,Xu, R.M.,Rao, Z.,Liu, Y. (deposition date: 2006-10-16, release date: 2007-06-26, Last modification date: 2024-03-13)

Primary citation

Yang, X.,Zhou, J.,Sun, L.,Wei, Z.,Gao, J.,Gong, W.,Xu, R.M.,Rao, Z.,Liu, Y.
Structural basis for the function of DCN-1 in protein Neddylation.
J.Biol.Chem., 282:24490-24494, 2007

PubMed Abstract: Covalent modification by Nedd8 (neddylation) stimulates the ubiquitin-protein isopeptide ligase (E3) activities of Cullins. DCN-1, an evolutionarily conserved protein, promotes neddylation of Cullins in vivo, binds directly to Nedd8, and associates with Cdc53 in the budding yeast Saccharomyces cerevisiae. The 1.9A resolution structure of yeast DCN-1 shows that the region encompassing residues 66-269 has a rectangular parallelepiped-like all alpha-helical structures, consisting of an EF-hand motif N-terminal domain and a closely juxtaposed C-terminal domain with six alpha-helices. The EF-hand motif structure is highly similar to that of the c-Cbl ubiquitin E3 ligase. We also demonstrate that DCN-1 directly binds to Rbx-1, a factor important for protein neddylation. The structural and biochemical results are consistent with the role of DCN-1 as a scaffold protein in a multisubunit neddylation E3 ligase complex.

PubMed: 17597076
DOI: 10.1074/jbc.C700038200

Experimental method

X-RAY DIFFRACTION (1.92 Å)