3bq3
From Proteopedia
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|PDB= 3bq3 |SIZE=350|CAPTION= <scene name='initialview01'>3bq3</scene>, resolution 1.90Å | |PDB= 3bq3 |SIZE=350|CAPTION= <scene name='initialview01'>3bq3</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+1'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+1'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= DCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= DCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bq3 OCA], [http://www.ebi.ac.uk/pdbsum/3bq3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bq3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Chou, Y C.]] | [[Category: Chou, Y C.]] | ||
[[Category: Sicheri, F.]] | [[Category: Sicheri, F.]] | ||
| - | [[Category: GOL]] | ||
[[Category: cell cycle]] | [[Category: cell cycle]] | ||
| - | [[Category: cullin]] | ||
[[Category: e2]] | [[Category: e2]] | ||
[[Category: e3 ligase]] | [[Category: e3 ligase]] | ||
| Line 33: | Line 34: | ||
[[Category: neddylation]] | [[Category: neddylation]] | ||
[[Category: protein degradation]] | [[Category: protein degradation]] | ||
| - | [[Category: scf]] | ||
[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
| - | [[Category: ubiquitination]] | + | [[Category: ubiquitination,scf,cullin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:28:13 2008'' |
Revision as of 02:28, 31 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Gene: | DCN1 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of S. cerevisiae Dcn1
Overview
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.
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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