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| | <SX load='6rwa' size='340' side='right' viewer='molstar' caption='[[6rwa]], [[Resolution|resolution]] 4.00Å' scene=''> | | <SX load='6rwa' size='340' side='right' viewer='molstar' caption='[[6rwa]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rwa]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29999 Atcc 29999]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RWA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RWA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rwa]] 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=6RWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RWA FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rw6|6rw6]], [[6rw8|6rw8]], [[6rw9|6rw9]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcdA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29488 ATCC 29999])</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=6rwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwa OCA], [https://pdbe.org/6rwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rwa RCSB], [https://www.ebi.ac.uk/pdbsum/6rwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwa ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rwa OCA], [http://pdbe.org/6rwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rwa RCSB], [http://www.ebi.ac.uk/pdbsum/6rwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rwa ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8GF92_PHOLU Q8GF92_PHOLU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Atcc 29999]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Benz, R]] | + | [[Category: Photorhabdus luminescens]] |
| - | [[Category: Gatsogiannis, C]] | + | [[Category: Benz R]] |
| - | [[Category: Leidreiter, F]] | + | [[Category: Gatsogiannis C]] |
| - | [[Category: Meusch, D]] | + | [[Category: Leidreiter F]] |
| - | [[Category: Raunser, S]] | + | [[Category: Meusch D]] |
| - | [[Category: Roderer, D]] | + | [[Category: Raunser S]] |
| - | [[Category: Complex]]
| + | [[Category: Roderer D]] |
| - | [[Category: Membrane permeation]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Translocation]]
| + | |
| Structural highlights
Function
Q8GF92_PHOLU
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leidreiter F, Roderer D, Meusch D, Gatsogiannis C, Benz R, Raunser S. Common architecture of Tc toxins from human and insect pathogenic bacteria. Sci Adv. 2019 Oct 16;5(10):eaax6497. doi: 10.1126/sciadv.aax6497. eCollection, 2019 Oct. PMID:31663026 doi:http://dx.doi.org/10.1126/sciadv.aax6497
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