View source for 6yey


==Xenorhabdus nematophila XptA1 in complex with porcine mucosa heparin==
<StructureSection load='6yey' size='340' side='right'caption='[[6yey]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6yey]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenorhabdus_nematophila Xenorhabdus nematophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YEY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YEY 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]] 3.7&#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=6yey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yey OCA], [https://pdbe.org/6yey PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yey RCSB], [https://www.ebi.ac.uk/pdbsum/6yey PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yey ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Toxin complex (Tc) toxins are virulence factors of pathogenic bacteria. Tcs are composed of three subunits: TcA, TcB and TcC. TcA facilitates receptor-toxin interaction and membrane permeation, TcB and TcC form a toxin-encapsulating cocoon. While the mechanisms of holotoxin assembly and pore formation have been described, little is known about receptor binding of TcAs. Here, we identify heparins/heparan sulfates and Lewis antigens as receptors for different TcAs from insect and human pathogens. Glycan array screening reveals that all tested TcAs bind negatively charged heparins. Cryo-EM structures of Morganella morganii TcdA4 and Xenorhabdus nematophila XptA1 reveal that heparins/heparan sulfates unexpectedly bind to different regions of the shell domain, including receptor-binding domains. In addition, Photorhabdus luminescens TcdA1 binds to Lewis antigens with micromolar affinity. Here, the glycan interacts with the receptor-binding domain D of the toxin. Our results suggest a glycan dependent association mechanism of Tc toxins on the host cell surface.

Glycan-dependent cell adhesion mechanism of Tc toxins.,Roderer D, Brocker F, Sitsel O, Kaplonek P, Leidreiter F, Seeberger PH, Raunser S Nat Commun. 2020 Jun 1;11(1):2694. doi: 10.1038/s41467-020-16536-7. PMID:32483155<ref>PMID:32483155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6yey" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Xenorhabdus nematophila]]
[[Category: Broecker F]]
[[Category: Kaplonek P]]
[[Category: Leidreiter F]]
[[Category: Raunser S]]
[[Category: Roderer D]]
[[Category: Seeberger PH]]
[[Category: Sitsel O]]