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3bq3

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[[Image:3bq3.jpg|left|200px]]<br /><applet load="3bq3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3bq3.jpg|left|200px]]
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caption="3bq3, resolution 1.90&Aring;" />
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'''Crystal structure of S. cerevisiae Dcn1'''<br />
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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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|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>
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|ACTIVITY=
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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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}}
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'''Crystal structure of S. cerevisiae Dcn1'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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3BQ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Residue+A+1'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BQ3 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18206966 18206966]
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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]]
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[[Category: e3 ligases]]
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[[Category: e3 ligase]]
[[Category: ligase]]
[[Category: ligase]]
[[Category: nedd8]]
[[Category: nedd8]]
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[[Category: ubiquitination]]
[[Category: ubiquitination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:07:06 2008''
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''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

Image:3bq3.jpg


PDB ID 3bq3

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites:
Ligands:
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

Page seeded by OCA on Thu Mar 20 19:00:37 2008

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