6rw8: Difference between revisions

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'''Unreleased structure'''


The entry 6rw8 is ON HOLD
==Cryo-EM structure of Xenorhabdus nematophila XptA1==
<SX load='6rw8' size='340' side='right' viewer='molstar' caption='[[6rw8]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rw8]] 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=6RW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RW8 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]] 2.84&#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=6rw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rw8 OCA], [https://pdbe.org/6rw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rw8 RCSB], [https://www.ebi.ac.uk/pdbsum/6rw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rw8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D3VHH9_XENNA D3VHH9_XENNA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tc toxins use a syringe-like mechanism to penetrate the membrane and translocate toxic enzymes into the host cytosol. They are composed of three components: TcA, TcB, and TcC. Low-resolution structures of TcAs from different bacteria suggest a considerable difference in their architecture and possibly in their mechanism of action. Here, we present high-resolution structures of five TcAs from insect and human pathogens, which show a similar overall composition and domain organization. Essential structural features, including a trefoil protein knot, are present in all TcAs, suggesting a common mechanism of action. All TcAs form functional pores and can be combined with TcB-TcC subunits from other species to form active chimeric holotoxins. We identified a conserved ionic pair that stabilizes the shell, likely operating as a strong latch that only springs open after destabilization of other regions. Our results provide new insights into the architecture and mechanism of the Tc toxin family.


Authors:  
Common architecture of Tc toxins from human and insect pathogenic bacteria.,Leidreiter F, Roderer D, Meusch D, Gatsogiannis C, Benz R, Raunser S Sci Adv. 2019 Oct 16;5(10):eaax6497. doi: 10.1126/sciadv.aax6497. eCollection, 2019 Oct. PMID:31663026<ref>PMID:31663026</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6rw8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Xenorhabdus nematophila]]
[[Category: Benz R]]
[[Category: Gatsogiannis C]]
[[Category: Leidreiter F]]
[[Category: Meusch D]]
[[Category: Raunser S]]
[[Category: Roderer D]]
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