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3bq3

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[[Image:3bq3.jpg|left|200px]]
 
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==Crystal structure of S. cerevisiae Dcn1==
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The line below this paragraph, containing "STRUCTURE_3bq3", creates the "Structure Box" on the page.
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<StructureSection load='3bq3' size='340' side='right'caption='[[3bq3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3bq3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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>
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</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></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3bq3| PDB=3bq3 | SCENE= }}
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCN1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<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>
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'''Crystal structure of S. cerevisiae Dcn1'''
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/DCN1_YEAST DCN1_YEAST]] Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with HRT1/RBX1 to recruit the Nedd8-charged E2 UBC12 to the cullin component of SCF-type complexes.<ref>PMID:15988528</ref>
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==Overview==
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bq/3bq3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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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==About this Structure==
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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:18206966<ref>PMID:18206966</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Saccharomyces cerevisiae]]
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<div class="pdbe-citations 3bq3" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Chou, Y C.]]
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<references/>
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[[Category: Sicheri, F.]]
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__TOC__
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</StructureSection>
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[[Category: Atcc 18824]]
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[[Category: Large Structures]]
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[[Category: Chou, Y C]]
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[[Category: Sicheri, F]]
[[Category: Cell cycle]]
[[Category: Cell cycle]]
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[[Category: Cullin]]
[[Category: E2]]
[[Category: E2]]
[[Category: E3 ligase]]
[[Category: E3 ligase]]
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[[Category: Neddylation]]
[[Category: Neddylation]]
[[Category: Protein degradation]]
[[Category: Protein degradation]]
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[[Category: Scf]]
[[Category: Ubiquitin]]
[[Category: Ubiquitin]]
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[[Category: Ubiquitination,scf,cullin]]
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[[Category: Ubiquitination]]
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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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Current revision

Crystal structure of S. cerevisiae Dcn1

PDB ID 3bq3

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