2i1a: Difference between revisions

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[[Image:2i1a.png|left|200px]]


{{STRUCTURE_2i1a|  PDB=2i1a  |  SCENE=  }}
==A Retroviral Protease-Like Domain in the Eukaryotic Protein Ddi1==
 
<StructureSection load='2i1a' size='340' side='right'caption='[[2i1a]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
===A Retroviral Protease-Like Domain in the Eukaryotic Protein Ddi1===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2i1a]] is a 4 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=2I1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I1A FirstGlance]. <br>
{{ABSTRACT_PUBMED_17010377}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=2i1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i1a OCA], [https://pdbe.org/2i1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i1a RCSB], [https://www.ebi.ac.uk/pdbsum/2i1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i1a ProSAT]</span></td></tr>
==About this Structure==
</table>
[[2i1a]] is a 4 chain structure with 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=2I1A OCA].  
== Function ==
 
[https://www.uniprot.org/uniprot/DDI1_YEAST DDI1_YEAST] Acts as a linker between the 19S proteasome and polyubiquitinated proteins like the HO endonuclease and UFO1 via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control. Appears to act as negative regulator of constitutive exocytosis. May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly.<ref>PMID:10330187</ref> <ref>PMID:11238935</ref> <ref>PMID:12051757</ref> <ref>PMID:12925750</ref> <ref>PMID:15964793</ref> <ref>PMID:17144915</ref> <ref>PMID:16478980</ref>
==Reference==
== Evolutionary Conservation ==
<ref group="xtra">PMID:017010377</ref><references group="xtra"/>
[[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/i1/2i1a_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=2i1a ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Fass, D.]]
[[Category: Fass D]]
[[Category: Sirkis, R.]]
[[Category: Sirkis R]]
[[Category: Acid protease fold]]
[[Category: Dimer]]
[[Category: Protein turnover]]
[[Category: Retroviral protease domain]]