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1tgz

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[[Image:1tgz.gif|left|200px]]
 
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{{Structure
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==Structure of human Senp2 in complex with SUMO-1==
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|PDB= 1tgz |SIZE=350|CAPTION= <scene name='initialview01'>1tgz</scene>, resolution 2.80&Aring;
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<StructureSection load='1tgz' size='340' side='right'caption='[[1tgz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1tgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TGZ FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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|GENE= SENP2, KIAA1331 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), UBL1, SMT3H3, SMT3C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgz OCA], [https://pdbe.org/1tgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tgz RCSB], [https://www.ebi.ac.uk/pdbsum/1tgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tgz ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1th0|1TH0]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgz OCA], [http://www.ebi.ac.uk/pdbsum/1tgz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tgz RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/SENP2_HUMAN SENP2_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. May down-regulate CTNNB1 levels and thereby modulate the Wnt pathway (By similarity).<ref>PMID:12192048</ref> <ref>PMID:11896061</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tg/1tgz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tgz ConSurf].
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<div style="clear:both"></div>
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'''Structure of human Senp2 in complex with SUMO-1'''
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==See Also==
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*[[SUMO 3D Structures|SUMO 3D Structures]]
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*[[Sentrin-specific protease|Sentrin-specific protease]]
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==Overview==
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== References ==
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Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 revealed differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions. Further biochemical characterization of the three SUMO isoforms into which an additional Gly-Gly di-peptide was inserted, or whereby the respective SUMO tails from the three isoforms were swapped, suggests a strict dependence for SUMO isopeptidase activity on residues C-terminal to the conserved Gly-Gly motif and preferred cleavage site for SUMO proteases.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1TGZ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGZ OCA].
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==Reference==
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A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex., Reverter D, Lima CD, Structure. 2004 Aug;12(8):1519-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15296745 15296745]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Lima, C D.]]
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[[Category: Lima CD]]
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[[Category: Reverter, D.]]
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[[Category: Reverter D]]
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[[Category: axam]]
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[[Category: protease]]
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[[Category: senp]]
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[[Category: sumo]]
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[[Category: ulp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:53 2008''
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Current revision

Structure of human Senp2 in complex with SUMO-1

PDB ID 1tgz

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