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{{STRUCTURE_2vrr|  PDB=2vrr  |  SCENE=  }}
===STRUCTURE OF SUMO MODIFIED UBC9===
{{ABSTRACT_PUBMED_18691969}}


==Function==
==Structure of SUMO modified Ubc9==
[[http://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE]] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref><ref>PMID:17187077</ref>  
<StructureSection load='2vrr' size='340' side='right'caption='[[2vrr]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vrr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRR 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]] 2.22&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2vrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrr OCA], [https://pdbe.org/2vrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrr RCSB], [https://www.ebi.ac.uk/pdbsum/2vrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref> <ref>PMID:17187077</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/vr/2vrr_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=2vrr ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. Here we show that autosumoylation of the mammalian E2-conjugating enzyme Ubc9 at Lys14 regulates target discrimination. While not altering its activity toward HDAC4, E2-25K, PML, or TDG, sumoylation of Ubc9 impairs its activity on RanGAP1 and strongly activates sumoylation of the transcriptional regulator Sp100. Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that creates an additional interface with the SUMO conjugated to the E2, a mechanism distinct from Ubc9 approximately SUMO thioester recruitment. The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.


==About this Structure==
Ubc9 sumoylation regulates SUMO target discrimination.,Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A Mol Cell. 2008 Aug 8;31(3):371-82. PMID:18691969<ref>PMID:18691969</ref>
[[2vrr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRR OCA].
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vrr" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[SUMO|SUMO]]
*[[SUMO 3D Structures|SUMO 3D Structures]]
*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018691969</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Ubiquitin--protein ligase]]
[[Category: Fish A]]
[[Category: Dijk, W J.Van.]]
[[Category: Flotho A]]
[[Category: Fish, A.]]
[[Category: Johnson ES]]
[[Category: Flotho, A.]]
[[Category: Klug H]]
[[Category: Johnson, E S.]]
[[Category: Knipscheer P]]
[[Category: Klug, H.]]
[[Category: Mann M]]
[[Category: Knipscheer, P.]]
[[Category: Olsen JV]]
[[Category: Mann, M.]]
[[Category: Pichler A]]
[[Category: Olsen, J V.]]
[[Category: Sixma TK]]
[[Category: Pichler, A.]]
[[Category: Van Dijk WJ]]
[[Category: Sixma, T K.]]
[[Category: Cell cycle]]
[[Category: Cell cycle-ligase complex]]
[[Category: Cell cycle/ligase]]
[[Category: Cell division]]
[[Category: Chromosome partition]]
[[Category: Developmental protein]]
[[Category: E2]]
[[Category: Host-virus interaction]]
[[Category: Isopeptide bond]]
[[Category: Ligase]]
[[Category: Membrane]]
[[Category: Mitosis]]
[[Category: Modification]]
[[Category: Nucleus]]
[[Category: Phosphoprotein]]
[[Category: Posttranslational modification]]
[[Category: Sumo]]
[[Category: Ubc9]]
[[Category: Ubiquitin like molecule]]
[[Category: Ubl conjugation pathway]]

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