This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3bq3
From Proteopedia
| Line 4: | Line 4: | ||
|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> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[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
| |||||||
| , 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
Page seeded by OCA on Mon Mar 31 05:28:13 2008
