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| | ==Crystal structure of deSUMOylase(DUF862)== | | ==Crystal structure of deSUMOylase(DUF862)== |
| - | <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 [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WP7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wp7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wp7 OCA], [http://pdbe.org/2wp7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wp7 RCSB], [http://www.ebi.ac.uk/pdbsum/2wp7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wp7 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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 == |
| - | [[http://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> | + | [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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Kim, J H]] | + | [[Category: Mus musculus]] |
| - | [[Category: Oh, B H]] | + | [[Category: Kim JH]] |
| - | [[Category: Woo, J S]] | + | [[Category: Oh BH]] |
| - | [[Category: Hydrolase]] | + | [[Category: Woo JS]] |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Ubiquitin-like protein]]
| + | |
| 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 PubMed
Post-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
- ↑ Shin EJ, Shin HM, Nam E, Kim WS, Kim JH, Oh BH, Yun Y. DeSUMOylating isopeptidase: a second class of SUMO protease. EMBO Rep. 2012 Apr;13(4):339-46. doi: 10.1038/embor.2012.3. PMID:22370726 doi:http://dx.doi.org/10.1038/embor.2012.3
- ↑ Suh HY, Kim JH, Woo JS, Ku B, Shin EJ, Yun Y, Oh BH. Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily. Proteins. 2012 Apr 13. doi: 10.1002/prot.24093. PMID:22498933 doi:10.1002/prot.24093
- ↑ Suh HY, Kim JH, Woo JS, Ku B, Shin EJ, Yun Y, Oh BH. Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative isopeptidase superfamily. Proteins. 2012 Apr 13. doi: 10.1002/prot.24093. PMID:22498933 doi:10.1002/prot.24093
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