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1vjv
From Proteopedia
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| - | [[Image:1vjv.gif|left|200px]] | ||
| - | + | ==Crystal structure of Ubiquitin carboxyl-terminal hydrolase 6 (yfr010w) from Saccharomyces cerevisiae at 1.74 A resolution== | |
| - | + | <StructureSection load='1vjv' size='340' side='right'caption='[[1vjv]], [[Resolution|resolution]] 1.74Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1vjv]] 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=1VJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VJV FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1vjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjv OCA], [https://pdbe.org/1vjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vjv RCSB], [https://www.ebi.ac.uk/pdbsum/1vjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vjv ProSAT], [https://www.topsan.org/Proteins/JCSG/1vjv TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/UBP6_YEAST UBP6_YEAST] Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5.<ref>PMID:9344467</ref> <ref>PMID:10527495</ref> <ref>PMID:12408819</ref> <ref>PMID:14581483</ref> <ref>PMID:17018280</ref> <ref>PMID:17190603</ref> | |
| - | + | == 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/vj/1vjv_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1vjv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Single protein]] | ||
| - | [[Category: Ubiquitin thiolesterase]] | ||
| - | [[Category: JCSG, Joint Center for Structural Genomics.]] | ||
| - | [[Category: jcsg]] | ||
| - | [[Category: joint center for structural genomic]] | ||
| - | [[Category: protein structure initiative]] | ||
| - | [[Category: psi]] | ||
| - | [[Category: structural genomic]] | ||
| - | [[Category: ubiquitin carboxyl-terminal hydrolase 6]] | ||
| - | [[Category: yfr010w]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:38 2008'' | ||
Current revision
Crystal structure of Ubiquitin carboxyl-terminal hydrolase 6 (yfr010w) from Saccharomyces cerevisiae at 1.74 A resolution
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