2wp7: Difference between revisions

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[[Image:2wp7.png|left|200px]]
==Crystal structure of deSUMOylase(DUF862)==
<StructureSection load='2wp7' size='340' side='right' caption='[[2wp7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wp7]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WP7 FirstGlance]. <br>
</td></tr><tr><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://www.rcsb.org/pdb/explore.do?structureId=2wp7 RCSB], [http://www.ebi.ac.uk/pdbsum/2wp7 PDBsum]</span></td></tr>
<table>
== 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/wp/2wp7_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


{{STRUCTURE_2wp7|  PDB=2wp7  |  SCENE=  }}
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<ref>PMID:22498933</ref>


===Crystal structure of deSUMOylase(DUF862)===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_22498933}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2wp7]] is a 1 chain structure with sequence from [http://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].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:022498933</ref><references group="xtra"/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Kim, J H.]]
[[Category: Kim, J H.]]

Revision as of 12:50, 21 May 2014

Crystal structure of deSUMOylase(DUF862)Crystal structure of deSUMOylase(DUF862)

Structural highlights

2wp7 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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

2wp7, resolution 1.90Å

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