6w9o

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(New page: '''Unreleased structure''' The entry 6w9o is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures)
Current revision (14:19, 18 October 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6w9o is ON HOLD until Paper Publication
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==Crystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel==
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<StructureSection load='6w9o' size='340' side='right'caption='[[6w9o]], [[Resolution|resolution]] 1.47&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 1.47&#8491;</td></tr>
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<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>
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q73HU7_WOLPM Q73HU7_WOLPM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6w9o" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Wolbachia endosymbiont of Drosophila melanogaster]]
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[[Category: Komander D]]
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[[Category: Pruneda JN]]
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[[Category: Schubert AF]]

Current revision

Crystal structure of an OTU deubiquitinase from Wolbachia pipientis wMel

PDB ID 6w9o

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