3bq3: Difference between revisions

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New page: left|200px<br /><applet load="3bq3" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bq3, resolution 1.90Å" /> '''Crystal structure of...
 
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[[Image:3bq3.jpg|left|200px]]<br /><applet load="3bq3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="3bq3, resolution 1.90&Aring;" />
'''Crystal structure of S. cerevisiae Dcn1'''<br />


==Overview==
==Crystal structure of S. cerevisiae Dcn1==
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.
<StructureSection load='3bq3' size='340' side='right'caption='[[3bq3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bq3]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BQ3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bq3 OCA], [https://pdbe.org/3bq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bq3 RCSB], [https://www.ebi.ac.uk/pdbsum/3bq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bq3 ProSAT]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/3bq3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bq3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:18206966</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 3bq3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Chou YC]]
[[Category: Chou, Y.C.]]
[[Category: Sicheri F]]
[[Category: Sicheri, F.]]
[[Category: GOL]]
[[Category: cell cycle]]
[[Category: cullin]]
[[Category: e2]]
[[Category: e3 ligases]]
[[Category: ligase]]
[[Category: nedd8]]
[[Category: neddylation]]
[[Category: protein degradation]]
[[Category: scf]]
[[Category: ubiquitin]]
[[Category: ubiquitination]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 11:04:16 2008''