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3bq3

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[[Image:3bq3.jpg|left|200px]]
[[Image:3bq3.jpg|left|200px]]
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{{Structure
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|PDB= 3bq3 |SIZE=350|CAPTION= <scene name='initialview01'>3bq3</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_3bq3", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+1'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|GENE= DCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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{{STRUCTURE_3bq3| PDB=3bq3 | SCENE= }}
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|RELATEDENTRY=
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|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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'''Crystal structure of S. cerevisiae Dcn1'''
'''Crystal structure of S. cerevisiae Dcn1'''
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[[Category: Chou, Y C.]]
[[Category: Chou, Y C.]]
[[Category: Sicheri, F.]]
[[Category: Sicheri, F.]]
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[[Category: cell cycle]]
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[[Category: Cell cycle]]
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[[Category: e2]]
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[[Category: E2]]
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[[Category: e3 ligase]]
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[[Category: E3 ligase]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: nedd8]]
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[[Category: Nedd8]]
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[[Category: neddylation]]
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[[Category: Neddylation]]
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[[Category: protein degradation]]
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[[Category: Protein degradation]]
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[[Category: ubiquitin]]
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[[Category: Ubiquitin]]
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[[Category: ubiquitination,scf,cullin]]
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[[Category: Ubiquitination,scf,cullin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:00:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:28:13 2008''
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Revision as of 18:00, 4 May 2008

Template:STRUCTURE 3bq3

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 Sun May 4 21:00:02 2008

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