8hm4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:01, 30 October 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 8hm4 is ON HOLD until Paper Publication
+
==Crystal structure of PPIase==
 +
<StructureSection load='8hm4' size='340' side='right'caption='[[8hm4]], [[Resolution|resolution]] 3.79&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[8hm4]] is a 2 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=8HM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HM4 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]] 3.79&#8491;</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=8hm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hm4 OCA], [https://pdbe.org/8hm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hm4 RCSB], [https://www.ebi.ac.uk/pdbsum/8hm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hm4 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/A0A0K6BYR7_BACFG A0A0K6BYR7_BACFG]
 +
<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: Crystal structure of PPIase
+
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 8hm4" 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]]

Current revision

Crystal structure of PPIase

PDB ID 8hm4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools