3bq3: Difference between revisions
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[[Image:3bq3.jpg|left|200px]] | [[Image:3bq3.jpg|left|200px]] | ||
'''Crystal structure of S. cerevisiae Dcn1''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= DCN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Crystal structure of S. cerevisiae Dcn1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3BQ3 is a [ | 3BQ3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BQ3 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18206966 18206966] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cullin]] | [[Category: cullin]] | ||
[[Category: e2]] | [[Category: e2]] | ||
[[Category: e3 | [[Category: e3 ligase]] | ||
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: nedd8]] | [[Category: nedd8]] | ||
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[[Category: ubiquitination]] | [[Category: ubiquitination]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:00:37 2008'' | ||
Revision as of 17:00, 20 March 2008
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| 3bq3, resolution 1.90Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Sites: | AC1 | ||||||||||||
| Ligands: | GOL | ||||||||||||
| Gene: | DCN1 (Saccharomyces cerevisiae) | ||||||||||||
| 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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