View source for 8cp6


==Type six secretion system exported effector 5 (Tse5)==
<StructureSection load='8cp6' size='340' side='right'caption='[[8cp6]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cp6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CP6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.45&#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=8cp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cp6 OCA], [https://pdbe.org/8cp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cp6 RCSB], [https://www.ebi.ac.uk/pdbsum/8cp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cp6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TSE5_PSEAE TSE5_PSEAE] Toxin secreted by the H1 type VI (H1-T6SS) secretion system that acts on bacterial target cells. The producing bacterium is protected by a cognate immunity protein.<ref>PMID:24589350</ref> <ref>PMID:24794869</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial competition is a significant driver of toxin polymorphism, which allows continual compensatory evolution between toxins and the resistance developed to overcome their activity. Bacterial Rearrangement hot spot (Rhs) proteins represent a widespread example of toxin polymorphism. Here, we present the 2.45 A cryo-electron microscopy structure of Tse5, an Rhs protein central to Pseudomonas aeruginosa type VI secretion system-mediated bacterial competition. This structural insight, coupled with an extensive array of biophysical and genetic investigations, unravels the multifaceted functional mechanisms of Tse5. The data suggest that interfacial Tse5-membrane binding delivers its encapsulated pore-forming toxin fragment to the target bacterial membrane, where it assembles pores that cause cell depolarisation and, ultimately, bacterial death.

Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane.,Gonzalez-Magana A, Tascon I, Altuna-Alvarez J, Queralt-Martin M, Colautti J, Velazquez C, Zabala M, Rojas-Palomino J, Cardenas M, Alcaraz A, Whitney JC, Ubarretxena-Belandia I, Albesa-Jove D Nat Commun. 2023 Nov 28;14(1):7808. doi: 10.1038/s41467-023-43585-5. PMID:38016939<ref>PMID:38016939</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8cp6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Albesa-Jove D]]
[[Category: Gonzalez-Magana A]]
[[Category: Tascon I]]
[[Category: Ubarretxena-Belandia I]]