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| | ==Cryo-EM structure of Photorhabdus luminescens TcdA1== | | ==Cryo-EM structure of Photorhabdus luminescens TcdA1== |
| - | <StructureSection load='6rw6' size='340' side='right'caption='[[6rw6]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <SX load='6rw6' size='340' side='right' viewer='molstar' caption='[[6rw6]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rw6]] 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=6RW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RW6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rw6]] 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=6RW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RW6 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcdA, tcdA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29488 ATCC 29999])</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]] 2.75Å</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=6rw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rw6 OCA], [http://pdbe.org/6rw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rw6 RCSB], [http://www.ebi.ac.uk/pdbsum/6rw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rw6 ProSAT]</span></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=6rw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rw6 OCA], [https://pdbe.org/6rw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rw6 RCSB], [https://www.ebi.ac.uk/pdbsum/6rw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rw6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9RN43_PHOLU Q9RN43_PHOLU] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </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
Q9RN43_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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