8zht
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of PpiD-YfgM complex== | |
| + | <StructureSection load='8zht' size='340' side='right'caption='[[8zht]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8zht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ZHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZHT 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]] 3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8zht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zht OCA], [https://pdbe.org/8zht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zht RCSB], [https://www.ebi.ac.uk/pdbsum/8zht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zht ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0N7IAL9_BACT4 A0A0N7IAL9_BACT4] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Antagonistic interactions play a key role in determining microbial community dynamics. Here, we report that one of the most widespread contact-dependent effectors in human gut microbiomes, Bte1, directly targets the PpiD-YfgM periplasmic chaperone complex in related microbes. Structural, biochemical, and genetic characterization of this interaction reveals that Bte1 reverses the activity of the chaperone complex, promoting substrate aggregation and toxicity. Using Bacteroides, we show that Bte1 is active in the mammalian gut, conferring a fitness advantage to expressing strains. Recipient cells targeted by Bte1 exhibit sensitivity to membrane-compromising conditions, and human gut microbes can use this effector to exploit pathogen-induced inflammation in the gut. Further, Bte1 allelic variation in gut metagenomes provides evidence for an arms race between Bte1-encoding and immunity-encoding strains in humans. Together, these studies demonstrate that human gut microbes alter the protein-folding capacity of neighboring cells and suggest strategies for manipulating community dynamics. | ||
| - | + | A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.,Lim B, Xu J, Wierzbicki IH, Gonzalez CG, Chen Z, Gonzalez DJ, Gao X, Goodman AL Cell Host Microbe. 2025 Jan 29:S1931-3128(25)00026-5. doi: , 10.1016/j.chom.2025.01.008. PMID:39909037<ref>PMID:39909037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Chen | + | <div class="pdbe-citations 8zht" style="background-color:#fffaf0;"></div> |
| - | [[Category: Gao | + | == References == |
| - | [[Category: Xu | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacteroides thetaiotaomicron]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen Z]] | ||
| + | [[Category: Gao X]] | ||
| + | [[Category: Xu JH]] | ||
Current revision
Structure of PpiD-YfgM complex
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