Reference: Yang X, et al. (2007) Structural Basis for the Function of DCN-1 in Protein Neddylation. J Biol Chem 282(34):24490-4

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Abstract


Covalent modification by Nedd8 (neddylation) stimulates the ubiquitin E3 ligase 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 Sacchromyces cerevisiae. The 1.9 A-resolution structure of yeast DCN-1 shows that the region encompassing residues 66-269 has a rectangular parallelepiped-like all a-helical structure, consisting of an EF-hand motif N-terminal domain and a closely juxtaposed C-terminal domain with six a-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 DCN-1's role as a scaffold protein in a multi-subunit neddylation E3 ligase complex.

Reference Type
Journal Article
Authors
Yang X, Zhou J, Sun L, Wei Z, Gao J, Gong W, Xu RM, Rao Z, Liu Y
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