View source for 5lkh


==Cryo-EM structure of the Tc toxin TcdA1 in its pore state (obtained by flexible fitting)==
<SX load='5lkh' size='340' side='right' viewer='molstar' caption='[[5lkh]], [[Resolution|resolution]] 3.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lkh]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_luminescens Photorhabdus luminescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LKH 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]] 3.46&#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=5lkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lkh OCA], [https://pdbe.org/5lkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lkh RCSB], [https://www.ebi.ac.uk/pdbsum/5lkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lkh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9RN43_PHOLU Q9RN43_PHOLU] 
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== Publication Abstract from PubMed ==
Tc toxins from pathogenic bacteria use a special syringe-like mechanism to perforate the host cell membrane and inject a deadly enzyme into the host cytosol. The molecular mechanism of this unusual injection system is poorly understood. Using electron cryomicroscopy, we determined the structure of TcdA1 from Photorhabdus luminescens embedded in lipid nanodiscs. In our structure, compared with the previous structure of TcdA1 in the prepore state, the transmembrane helices rearrange in the membrane and open the initially closed pore. However, the helices do not span the complete membrane; instead, the loops connecting the helices form the rim of the funnel. Lipid head groups reach into the space between the loops and consequently stabilize the pore conformation. The linker domain is folded and packed into a pocket formed by the other domains of the toxin, thereby considerably contributing to stabilization of the pore state.

Membrane insertion of a Tc toxin in near-atomic detail.,Gatsogiannis C, Merino F, Prumbaum D, Roderer D, Leidreiter F, Meusch D, Raunser S Nat Struct Mol Biol. 2016 Aug 29. doi: 10.1038/nsmb.3281. PMID:27571177<ref>PMID:27571177</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5lkh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Photorhabdus luminescens]]
[[Category: Gatsogiannis C]]
[[Category: Leidreiter F]]
[[Category: Merino F]]
[[Category: Meusch D]]
[[Category: Prumbaum D]]
[[Category: Raunser S]]
[[Category: Roderer D]]