3rq9: Difference between revisions

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<StructureSection load='3rq9' size='340' side='right'caption='[[3rq9]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
<StructureSection load='3rq9' size='340' side='right'caption='[[3rq9]], [[Resolution|resolution]] 1.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3rq9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQ9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3rq9]] is a 2 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=3RQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQ9 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA2703 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1&#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=3rq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rq9 OCA], [https://pdbe.org/3rq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rq9 RCSB], [https://www.ebi.ac.uk/pdbsum/3rq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rq9 ProSAT]</span></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=3rq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rq9 OCA], [https://pdbe.org/3rq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rq9 RCSB], [https://www.ebi.ac.uk/pdbsum/3rq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rq9 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/TSI2_PSEAE TSI2_PSEAE] Immunity protein that plays a role in preventing early activation of toxin Tse2. Binds to a large surface of Tse2 and thereby occludes the active site to specifically inhibits Tse2.<ref>PMID:22310046</ref> <ref>PMID:22511866</ref> <ref>PMID:26749446</ref>  
The type VI secretion system (T6SS) has emerged as an important mediator of interbacterial interactions. A T6SS from Pseudomonas aeruginosa targets at least three effector proteins, type VI secretion exported 1-3 (Tse1-3), to recipient Gram-negative cells. The Tse2 protein is a cytoplasmic effector that acts as a potent inhibitor of target cell proliferation, thus providing a pronounced fitness advantage for P. aeruginosa donor cells. P. aeruginosa utilizes a dedicated immunity protein, type VI secretion immunity 2 (Tsi2), to protect against endogenous and intercellularly-transferred Tse2. Here we show that Tse2 delivered by the T6SS efficiently induces quiescence, not death, within recipient cells. We demonstrate that despite direct interaction of Tsi2 and Tse2 in the cytoplasm, Tsi2 is dispensable for targeting the toxin to the secretory apparatus. To gain insights into the molecular basis of Tse2 immunity, we solved the 1.00 A X-ray crystal structure of Tsi2. The structure shows that Tsi2 assembles as a dimer that does not resemble previously characterized immunity or antitoxin proteins. A genetic screen for Tsi2 mutants deficient in Tse2 interaction revealed an acidic patch distal to the Tsi2 homodimer interface that mediates toxin interaction and immunity. Consistent with this finding, we observed that destabilization of the Tsi2 dimer does not impact Tse2 interaction. The molecular insights into Tsi2 structure and function garnered from this study shed light on the mechanisms of T6 effector secretion, and indicate that the Tse2-Tsi2 effector-immunity pair has features distinguishing it from previously characterized toxin-immunity and toxin-antitoxin systems.
 
Structural Basis for Type VI Secretion Effector Recognition by a Cognate Immunity Protein.,Li M, Le Trong I, Carl MA, Larson ET, Chou S, De Leon JA, Dove SL, Stenkamp RE, Mougous JD PLoS Pathog. 2012 Apr;8(4):e1002613. Epub 2012 Apr 12. PMID:22511866<ref>PMID:22511866</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3rq9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Li, M]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Mougous, J D]]
[[Category: Le Trong I]]
[[Category: Stenkamp, R E]]
[[Category: Li M]]
[[Category: Trong, I Le]]
[[Category: Mougous JD]]
[[Category: Antitoxin]]
[[Category: Stenkamp RE]]
[[Category: Immunity protein]]
[[Category: T6]]
[[Category: Tse2-binding protein]]
[[Category: Type vi secretion]]
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