2wp7: Difference between revisions
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<StructureSection load='2wp7' size='340' side='right'caption='[[2wp7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='2wp7' size='340' side='right'caption='[[2wp7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2wp7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2wp7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WP7 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=2wp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wp7 OCA], [https://pdbe.org/2wp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wp7 RCSB], [https://www.ebi.ac.uk/pdbsum/2wp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wp7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/DESI1_MOUSE DESI1_MOUSE]] Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity. Desumoylates ZBTB46.<ref>PMID:22370726</ref> <ref>PMID:22498933</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 14:12, 6 April 2022
Crystal structure of deSUMOylase(DUF862)Crystal structure of deSUMOylase(DUF862)
Structural highlights
Function[DESI1_MOUSE] Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some substrate proteins. Has isopeptidase but not SUMO-processing activity. Desumoylates ZBTB46.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPost-translational modification by SUMO can be reversed by SENPs, the first known class of deSUMOylase. Recently, we identified a new deSUMOylating enzyme DeSI-1, which is distinct from SENPs and belongs to the putative deubiquitinating isopeptidase PPPDE superfamily. Herein, we report the crystal structure of DeSI-1, revealing that this enzyme forms a homodimer and that the groove between the two subunits is the active site harboring two absolutely conserved cysteine and histidine residues which form a catalytic dyad. We also show that DeSI-1 exhibits an extremely low endopeptidase activity toward precursor forms of SUMO-1 and SUMO-2, unlike SENPs. Proteins 2012. (c) 2012 Wiley-Liss, Inc. Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily.,Suh HY, Kim JH, Woo JS, Ku B, Shin EJ, Yun Y, Oh BH Proteins. 2012 Apr 13. doi: 10.1002/prot.24093. PMID:22498933[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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