|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4o9y' size='340' side='right'caption='[[4o9y]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='4o9y' size='340' side='right'caption='[[4o9y]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o9y]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29999 Atcc 29999]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vw1 1vw1] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vw2 1vw2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o9y]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Photorhabdus_luminescens Photorhabdus luminescens]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vw1 1vw1] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vw2 1vw2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O9Y FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o9x|4o9x]]</td></tr> | + | </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=4o9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9y OCA], [https://pdbe.org/4o9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o9y RCSB], [https://www.ebi.ac.uk/pdbsum/4o9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9y ProSAT]</span></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>
| + | |
| - | <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=4o9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9y OCA], [http://pdbe.org/4o9y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o9y RCSB], [http://www.ebi.ac.uk/pdbsum/4o9y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9y 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 == |
| Line 21: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 29999]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aktories, K]] | + | [[Category: Photorhabdus luminescens]] |
| - | [[Category: Efremov, R G]] | + | [[Category: Aktories K]] |
| - | [[Category: Gatsogiannis, C]] | + | [[Category: Efremov RG]] |
| - | [[Category: Hofnagel, O]] | + | [[Category: Gatsogiannis C]] |
| - | [[Category: Lang, A E]] | + | [[Category: Hofnagel O]] |
| - | [[Category: Meusch, D]] | + | [[Category: Lang AE]] |
| - | [[Category: Raunser, S]] | + | [[Category: Meusch D]] |
| - | [[Category: Vetter, I R]] | + | [[Category: Raunser S]] |
| - | [[Category: Pore-forming]]
| + | [[Category: Vetter IR]] |
| - | [[Category: Tc toxin]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
Q9RN43_PHOLU
Publication Abstract from PubMed
Tripartite Tc toxin complexes of bacterial pathogens perforate the host membrane and translocate toxic enzymes into the host cell, including in humans. The underlying mechanism is complex but poorly understood. Here we report the first, to our knowledge, high-resolution structures of a TcA subunit in its prepore and pore state and of a complete 1.7 megadalton Tc complex. The structures reveal that, in addition to a translocation channel, TcA forms four receptor-binding sites and a neuraminidase-like region, which are important for its host specificity. pH-induced opening of the shell releases an entropic spring that drives the injection of the TcA channel into the membrane. Binding of TcB/TcC to TcA opens a gate formed by a six-bladed beta-propeller and results in a continuous protein translocation channel, whose architecture and properties suggest a novel mode of protein unfolding and translocation. Our results allow us to understand key steps of infections involving Tc toxins at the molecular level.
Mechanism of Tc toxin action revealed in molecular detail.,Meusch D, Gatsogiannis C, Efremov RG, Lang AE, Hofnagel O, Vetter IR, Aktories K, Raunser S Nature. 2014 Apr 3;508(7494):61-5. doi: 10.1038/nature13015. Epub 2014 Feb 23. PMID:24572368[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Meusch D, Gatsogiannis C, Efremov RG, Lang AE, Hofnagel O, Vetter IR, Aktories K, Raunser S. Mechanism of Tc toxin action revealed in molecular detail. Nature. 2014 Apr 3;508(7494):61-5. doi: 10.1038/nature13015. Epub 2014 Feb 23. PMID:24572368 doi:http://dx.doi.org/10.1038/nature13015
|
