7bu0

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'''Unreleased structure'''
 
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The entry 7bu0 is ON HOLD until Apr 03 2022
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==Crystal structure of a OTU deubiquitinase in complex with Ub-PA==
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<StructureSection load='7bu0' size='340' side='right'caption='[[7bu0]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7bu0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BU0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</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=7bu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bu0 OCA], [https://pdbe.org/7bu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bu0 RCSB], [https://www.ebi.ac.uk/pdbsum/7bu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bu0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q5ZSI8_LEGPH Q5ZSI8_LEGPH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Legionella pneumophila extensively modulates the host ubiquitin network to create the Legionella-containing vacuole (LCV) for its replication. Many of its virulence factors function as ubiquitin ligases or deubiquitinases (DUBs). Here, we identify Lem27 as a DUB that displays a preference for diubiquitin formed by K6, K11, or K48. Lem27 is associated with the LCV where it regulates Rab10 ubiquitination in concert with SidC and SdcA, two bacterial E3 ubiquitin ligases. Structural analysis of the complex formed by an active fragment of Lem27 and the substrate-based suicide inhibitor ubiquitin-propargylamide (PA) reveals that it harbors a fold resembling those in the OTU1 DUB subfamily with a Cys-His catalytic dyad and that it recognizes ubiquitin via extensive hydrogen bonding at six contact sites. Our results establish Lem27 as a DUB that functions to regulate protein ubiquitination on L. pneumophila phagosomes by counteracting the activity of bacterial ubiquitin E3 ligases.
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Authors:
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Interplay between bacterial deubiquitinase and ubiquitin E3 ligase regulates ubiquitin dynamics on Legionella phagosomes.,Liu S, Luo J, Zhen X, Qiu J, Ouyang S, Luo ZQ Elife. 2020 Nov 2;9:e58114. doi: 10.7554/eLife.58114. PMID:33136002<ref>PMID:33136002</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 7bu0" 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: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
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[[Category: Ouyang SY]]
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[[Category: Zhen XK]]

Current revision

Crystal structure of a OTU deubiquitinase in complex with Ub-PA

PDB ID 7bu0

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