6w9o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:19, 18 October 2023) (edit) (undo)
 
Line 1: Line 1:
==Crystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel==
==Crystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel==
-
<StructureSection load='6w9o' size='340' side='right'caption='[[6w9o]]' scene=''>
+
<StructureSection load='6w9o' size='340' side='right'caption='[[6w9o]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W9O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W9O FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6w9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolbachia_endosymbiont_of_Drosophila_melanogaster Wolbachia endosymbiont of Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6W9O FirstGlance]. <br>
-
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w9o OCA], [http://pdbe.org/6w9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w9o RCSB], [http://www.ebi.ac.uk/pdbsum/6w9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w9o 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]] 1.47&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=6w9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w9o OCA], [https://pdbe.org/6w9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6w9o RCSB], [https://www.ebi.ac.uk/pdbsum/6w9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6w9o ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q73HU7_WOLPM Q73HU7_WOLPM]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Manipulation of host ubiquitin signaling is becoming an increasingly apparent evolutionary strategy among bacterial and viral pathogens. By removing host ubiquitin signals, for example, invading pathogens can inactivate immune response pathways and evade detection. The ovarian tumor (OTU) family of deubiquitinases regulates diverse ubiquitin signals in humans. Viral pathogens have also extensively co-opted the OTU fold to subvert host signaling, but the extent to which bacteria utilize the OTU fold was unknown. We have predicted and validated a set of OTU deubiquitinases encoded by several classes of pathogenic bacteria. Biochemical assays highlight the ubiquitin and polyubiquitin linkage specificities of these bacterial deubiquitinases. By determining the ubiquitin-bound structures of two examples, we demonstrate the novel strategies that have evolved to both thread an OTU fold and recognize a ubiquitin substrate. With these new examples, we perform the first cross-kingdom structural analysis of the OTU fold that highlights commonalities among distantly related OTU deubiquitinases.
 +
 +
Identification and characterization of diverse OTU deubiquitinases in bacteria.,Schubert AF, Nguyen JV, Franklin TG, Geurink PP, Roberts CG, Sanderson DJ, Miller LN, Ovaa H, Hofmann K, Pruneda JN, Komander D EMBO J. 2020 Jun 22:e105127. doi: 10.15252/embj.2020105127. PMID:32567101<ref>PMID:32567101</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 6w9o" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
 +
[[Category: Wolbachia endosymbiont of Drosophila melanogaster]]
[[Category: Komander D]]
[[Category: Komander D]]
[[Category: Pruneda JN]]
[[Category: Pruneda JN]]
[[Category: Schubert AF]]
[[Category: Schubert AF]]

Current revision

Crystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel

PDB ID 6w9o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools