6rwb

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'''Unreleased structure'''
 
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The entry 6rwb is ON HOLD until Paper Publication
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==Cryo-EM structure of Yersinia pseudotuberculosis TcaA-TcaB==
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<SX load='6rwb' size='340' side='right' viewer='molstar' caption='[[6rwb]], [[Resolution|resolution]] 3.25&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6rwb]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pseudotuberculosis Yersinia pseudotuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RWB FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.25&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6rwb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwb OCA], [https://pdbe.org/6rwb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rwb RCSB], [https://www.ebi.ac.uk/pdbsum/6rwb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwb ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6rwb" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Yersinia pseudotuberculosis]]
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[[Category: Benz R]]
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[[Category: Gatsogiannis C]]
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[[Category: Leidreiter F]]
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[[Category: Meusch D]]
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[[Category: Raunser S]]
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[[Category: Roderer D]]

Current revision

Cryo-EM structure of Yersinia pseudotuberculosis TcaA-TcaB

6rwb, resolution 3.25Å

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