View source for 9ils


==The GmvT toxin in complex with the C-terminal fragment of its antitoxin==
<StructureSection load='9ils' size='340' side='right'caption='[[9ils]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ils]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_sonnei Shigella sonnei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ILS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ILS 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]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=9ils FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ils OCA], [https://pdbe.org/9ils PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ils RCSB], [https://www.ebi.ac.uk/pdbsum/9ils PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ils ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Toxin-antitoxin (TA) systems are common bicistronic gene elements in bacteria and are critical for stress responses. The toxin members of the GNAT/RHH TA family can acetylate certain aminoacylated tRNA molecules and inhibit global protein translation. One member named GmvT is important for virulence plasmid maintenance in Shigella flexneri, but the underlying mechanism remains poorly understood. Here, we report the cocrystal structures of GmvT in two forms. The binding of the antitoxin mainly relies on the backbone of the toxin while the cofactor is free of contacts with the antitoxin, supported by follow-up in vitro and in vivo studies. Our study provides insight into the protein-protein/protein-ligand interactions of the GmvAT pair and the structural basis for molecular recognition.

Structural insights into the Shigella flexneri GmvAT toxin-antitoxin system.,Chen R, Zhao H, Zhou J, Liu A, Guo Y, Wu K, Xiang Y, Lei J, Jiang S, Xie W FEBS Lett. 2025 Feb 20. doi: 10.1002/1873-3468.70015. PMID:39973444<ref>PMID:39973444</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9ils" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Shigella sonnei]]
[[Category: Chen R]]
[[Category: Xie W]]
[[Category: Zhao H]]