3bq3

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(New page: 200px<br /><applet load="3bq3" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bq3, resolution 1.90&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==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 [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].
==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18206966 18206966]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chou, Y.C.]]
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[[Category: Chou, Y C.]]
[[Category: Sicheri, F.]]
[[Category: Sicheri, F.]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: ubiquitination]]
[[Category: ubiquitination]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:04:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:07:06 2008''

Revision as of 17:07, 21 February 2008

Image:3bq3.jpg

3bq3, resolution 1.90Å

Drag the structure with the mouse to rotate

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 with as ligand. Known structural/functional Site: . 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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