3eay: Difference between revisions
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==Crystal structure of the human SENP7 catalytic domain== | ==Crystal structure of the human SENP7 catalytic domain== | ||
<StructureSection load='3eay' size='340' side='right' caption='[[3eay]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3eay' size='340' side='right' caption='[[3eay]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SENP7, KIAA1707, SSP2, SUSP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SENP7, KIAA1707, SSP2, SUSP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3eay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eay OCA], [http://pdbe.org/3eay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eay RCSB], [http://www.ebi.ac.uk/pdbsum/3eay PDBsum]</span></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=3eay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eay OCA], [http://pdbe.org/3eay PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3eay RCSB], [http://www.ebi.ac.uk/pdbsum/3eay PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3eay ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3eay" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3eay" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Lima, C D]] | [[Category: Lima, C D]] | ||
[[Category: Reverter, D]] | [[Category: Reverter, D]] | ||
[[Category: Alternative splicing]] | |||
[[Category: Crystal]] | [[Category: Crystal]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
[[Category: Polymorphism]] | |||
[[Category: Protease]] | [[Category: Protease]] | ||
[[Category: Senp]] | [[Category: Senp]] | ||
Revision as of 12:07, 25 October 2017
Crystal structure of the human SENP7 catalytic domainCrystal structure of the human SENP7 catalytic domain
Structural highlights
Function[SENP7_HUMAN] Protease that deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full-length SUMO proteins to their mature forms.[1] 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 PubMedSmall ubiquitin-like modifier (SUMO) proteases regulate the abundance and lifetime of SUMO-conjugated substrates by antagonizing reactions catalyzed by SUMO-conjugating enzymes. Six SUMO proteases constitute the human SENP/ULP protease family (SENP1-3 and SENP5-7). SENP6 and SENP7 include the most divergent class of SUMO proteases, which also includes the yeast enzyme ULP2. We present the crystal structure of the SENP7 catalytic domain at a resolution of 2.4 angstroms. Comparison with structures of human SENP1 and SENP2 reveals unique elements that differ from previously characterized structures of SUMO-deconjugating enzymes. Biochemical assays show that SENP6 and SENP7 prefer SUMO2 or SUMO3 in deconjugation reactions with rates comparable with those catalyzed by SENP2, particularly during cleavage of di-SUMO2, di-SUMO3, and poly-SUMO chains composed of SUMO2 or SUMO3. In contrast, SENP6 and SENP7 exhibit lower rates for processing pre-SUMO1, pre-SUMO2, or pre-SUMO3 in comparison with SENP2. Structure-guided mutational analysis reveals elements unique to the SENP6 and SENP7 subclass of SENP/ULP proteases that contribute to protease function during deconjugation of poly-SUMO chains. Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7.,Lima CD, Reverter D J Biol Chem. 2008 Nov 14;283(46):32045-55. Epub 2008 Sep 16. PMID:18799455[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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