8hm3: Difference between revisions

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New page: '''Unreleased structure''' The entry 8hm3 is ON HOLD Authors: Xu, J.H., Chen, Z., Gao, X. Description: complex of PPIase-BfUbb Category: Unreleased Structures Category: Gao, X ...
 
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'''Unreleased structure'''


The entry 8hm3 is ON HOLD
==Complex of PPIase-BfUbb==
<StructureSection load='8hm3' size='340' side='right'caption='[[8hm3]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hm3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HM3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HM3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8hm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hm3 OCA], [https://pdbe.org/8hm3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hm3 RCSB], [https://www.ebi.ac.uk/pdbsum/8hm3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hm3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5L8M7_BACFN Q5L8M7_BACFN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interbacterial antagonism and associated defensive strategies are both essential during bacterial competition. The human gut symbiont Bacteroides fragilis secretes a ubiquitin homologue (BfUbb) that is toxic to a subset of B. fragilis strains in vitro. In the present study, we demonstrate that BfUbb lyses certain B. fragilis strains by non-covalently binding and inactivating an essential peptidyl-prolyl isomerase (PPIase). BfUbb-sensitivity profiling of B. fragilis strains revealed a key tyrosine residue (Tyr119) in the PPIase and strains that encode a glutamic acid residue at Tyr119 are resistant to BfUbb. Crystal structural analysis and functional studies of BfUbb and the BfUbb-PPIase complex uncover a unique disulfide bond at the carboxy terminus of BfUbb to mediate the interaction with Tyr119 of the PPIase. In vitro coculture assays and mouse studies show that BfUbb confers a competitive advantage for encoding strains and this is further supported by human gut metagenome analyses. Our findings reveal a previously undescribed mechanism of bacterial intraspecies competition.


Authors: Xu, J.H., Chen, Z., Gao, X.
Bacteroides fragilis ubiquitin homologue drives intraspecies bacterial competition in the gut microbiome.,Jiang K, Li W, Tong M, Xu J, Chen Z, Yang Y, Zang Y, Jiao X, Liu C, Lim B, Jiang X, Wang J, Wu D, Wang M, Liu SJ, Shao F, Gao X Nat Microbiol. 2024 Jan;9(1):70-84. doi: 10.1038/s41564-023-01541-5. Epub 2023 , Dec 11. PMID:38082149<ref>PMID:38082149</ref>


Description: complex of PPIase-BfUbb
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Gao, X]]
<div class="pdbe-citations 8hm3" style="background-color:#fffaf0;"></div>
[[Category: Chen, Z]]
== References ==
[[Category: Xu, J.H]]
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides fragilis]]
[[Category: Large Structures]]
[[Category: Chen Z]]
[[Category: Gao X]]
[[Category: Xu JH]]

Latest revision as of 07:21, 21 November 2024

Complex of PPIase-BfUbb

8hm3, resolution 2.26Å

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