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PDBsum entry 2is9

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Transcription PDB id
2is9
Contents
Protein chain
204 a.a.
Ligands
MES
Metals
_PT
_CL ×4
Waters ×168

References listed in PDB file
Key reference
Title Structural basis for the function of dcn-1 in protein neddylation.
Authors X.Yang, J.Zhou, L.Sun, Z.Wei, J.Gao, W.Gong, R.M.Xu, Z.Rao, Y.Liu.
Ref. J Biol Chem, 2007, 282, 24490-24494. [DOI no: 10.1074/jbc.C700038200]
PubMed id 17597076
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.
Figure 2.
Structure of DCN-1.A, a stereo ribbon diagram showing the overall structure of DCN-1. The structure is colored from the N to the C termini with blue to red. B, a surface representation of the DCN-1 structure. B1 (side 1) and B3 (side 2) show the distribution of conserved residues on the two sides of the protein surface. Absolutely conserved residues are indicated in blue, and highly conserved residues are shown in green, using the convention defined in the legend for Fig. 1. The arrow points to the position of Glu-260, which is colored in red. Electrostatic potential on the protein surface is shown in B2 and B4, which are oriented the same as in B1 and B3, respectively. Positively charged regions are shown in red, negatively charged regions are in blue, and neutral ones are in white.
Figure 3.
Superposition of c-Cbl and DCN-1.A, a stereo diagram of superimposed DCN-1 (blue) and c-Cbl (gray) EF-hand motifs. A red sphere represents a calcium ion bound to the c-Cbl EF-hand motif. B, superposition of c-Cbl (only EF-hand and helix bundle motifs are shown) with DCN-1 to show the different spatial arrangement of the two helix bundle motifs.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 24490-24494) copyright 2007.
PROCHECK
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