View source for 9vzo


==Crystal structure of ShosA from E. coli KTE181==
<StructureSection load='9vzo' size='340' side='right'caption='[[9vzo]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vzo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VZO 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]] 2.266927&#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=9vzo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vzo OCA], [https://pdbe.org/9vzo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vzo RCSB], [https://www.ebi.ac.uk/pdbsum/9vzo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vzo ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The ShosTA system, a two-component toxin-antitoxin (TA) system consisting of the ShosT and ShosA proteins, has recently been shown to mediate anti-phage defense. However, the molecular mechanisms underlying this system's role in anti-phage defense remain elusive. Here, we first confirmed that ShosT functions as the toxic component that induces cell death, while ShosA acts as the antitoxin to neutralize these toxic effects. We then solved the crystal structures of apo-ShosT, ShosA, and the ShosT-PRPP (phosphoribosyl pyrophosphate) complex. The structural data reveal that while ShosT contains a PRTase (phosphoribosyl-transferase) domain, it possesses unique noncanonical features; furthermore, we demonstrate that its binding to PRPP is indispensable for its toxic activity. ShosA is a DprA-like protein that functions as a homodimer. Both its ssDNA-binding and dimerization abilities are essential for its antitoxin activity. Further biochemical and structural studies demonstrate that ShosA directly binds to RecA, an interaction that is essential for neutralizing ShosT. The ShosA-RecA interaction is sensitive to the presence of ssDNA, implying that ShosTA-mediated abortive infection (Abi) may be triggered by the invading phage DNA. Our studies uncovered the mechanisms of ShosT inducing cell death and ShosA antagonizing the toxic effects of ShosT in anti-phage defense.

The molecular mechanisms of the ShosTA system in mediating anti-phage defense.,Yang R, He L, Wu Z, Wang R, Guo H, Yuan R, Su H, Chen G, Li F Nucleic Acids Res. 2026 Feb 24;54(5):gkag197. doi: 10.1093/nar/gkag197. PMID:41784268<ref>PMID:41784268</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vzo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: He L]]
[[Category: Li F]]
[[Category: Yang R]]