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| | <SX load='6rw8' size='340' side='right' viewer='molstar' caption='[[6rw8]], [[Resolution|resolution]] 2.84Å' scene=''> | | <SX load='6rw8' size='340' side='right' viewer='molstar' caption='[[6rw8]], [[Resolution|resolution]] 2.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rw8]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"achromobacter_nematophilus"_poinar_and_thomas_1965 "achromobacter nematophilus" poinar and thomas 1965]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RW8 FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rw6|6rw6]]</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]] 2.84Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xptA, XNC2_2467 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=628 "Achromobacter nematophilus" Poinar and Thomas 1965])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rw8 OCA], [http://pdbe.org/6rw8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rw8 RCSB], [http://www.ebi.ac.uk/pdbsum/6rw8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rw8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D3VHH9_XENNA D3VHH9_XENNA] |
| | <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: Achromobacter nematophilus poinar and thomas 1965]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Benz, R]] | + | [[Category: Xenorhabdus nematophila]] |
| - | [[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
D3VHH9_XENNA
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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