2vrr
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2vrr is ON HOLD until Paper Publication Authors: Knipscheer, P., Flotho, A., Klug, H., Olsen, J.V., van Dijk, W.J., Fish, A., Johnson, E.S., Mann, M...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of SUMO modified Ubc9== | |
| + | <StructureSection load='2vrr' size='340' side='right'caption='[[2vrr]], [[Resolution|resolution]] 2.22Å' 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]] 2.22Å</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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2vrr" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[SUMO 3D Structures|SUMO 3D Structures]] | |
| + | *[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Fish A]] | ||
| + | [[Category: Flotho A]] | ||
| + | [[Category: Johnson ES]] | ||
| + | [[Category: Klug H]] | ||
| + | [[Category: Knipscheer P]] | ||
| + | [[Category: Mann M]] | ||
| + | [[Category: Olsen JV]] | ||
| + | [[Category: Pichler A]] | ||
| + | [[Category: Sixma TK]] | ||
| + | [[Category: Van Dijk WJ]] | ||
Current revision
Structure of SUMO modified Ubc9
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Categories: Homo sapiens | Large Structures | Mus musculus | Fish A | Flotho A | Johnson ES | Klug H | Knipscheer P | Mann M | Olsen JV | Pichler A | Sixma TK | Van Dijk WJ
