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| | <StructureSection load='6r1j' size='340' side='right'caption='[[6r1j]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='6r1j' size='340' side='right'caption='[[6r1j]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6r1j]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeromonas_hydrophila_j-1 Aeromonas hydrophila j-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6R1J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6r1j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_hydrophila_J-1 Aeromonas hydrophila J-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6R1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6R1J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.92Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">V469_08880 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1419584 Aeromonas hydrophila J-1])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=6r1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r1j OCA], [http://pdbe.org/6r1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6r1j RCSB], [http://www.ebi.ac.uk/pdbsum/6r1j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6r1j 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=6r1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6r1j OCA], [https://pdbe.org/6r1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6r1j RCSB], [https://www.ebi.ac.uk/pdbsum/6r1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6r1j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0KLE2_AERHH A0KLE2_AERHH] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeromonas hydrophila j-1]] | + | [[Category: Aeromonas hydrophila J-1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baker, P J]] | + | [[Category: Baker PJ]] |
| - | [[Category: Churchill-Angus, A M]] | + | [[Category: Churchill-Angus AM]] |
| - | [[Category: Wilson, J S]] | + | [[Category: Wilson JS]] |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Tripartite pore-forming toxin]]
| + | |
| Structural highlights
Function
A0KLE2_AERHH
Publication Abstract from PubMed
The alpha helical CytolysinA family of pore forming toxins (alpha-PFT) contains single, two, and three component members. Structures of the single component Eschericia coli ClyA and the two component Yersinia enterolytica YaxAB show both undergo conformational changes from soluble to pore forms, and oligomerization to produce the active pore. Here we identify tripartite alpha-PFTs in pathogenic Gram negative bacteria, including Aeromonas hydrophila (AhlABC). We show that the AhlABC toxin requires all three components for maximal cell lysis. We present structures of pore components which describe a bi-fold hinge mechanism for soluble to pore transition in AhlB and a contrasting tetrameric assembly employed by soluble AhlC to hide their hydrophobic membrane associated residues. We propose a model of pore assembly where the AhlC tetramer dissociates, binds a single membrane leaflet, recruits AhlB promoting soluble to pore transition, prior to AhlA binding to form the active hydrophilic lined pore.
(Identification and structural analysis of the tripartite alpha-pore forming toxin of Aeromonas hydrophila).,Wilson JS, Churchill-Angus AM, Davies SP, Sedelnikova SE, Tzokov SB, Rafferty JB, Bullough PA, Bisson C, Baker PJ Nat Commun. 2019 Jul 1;10(1):2900. doi: 10.1038/s41467-019-10777-x. PMID:31263098[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wilson JS, Churchill-Angus AM, Davies SP, Sedelnikova SE, Tzokov SB, Rafferty JB, Bullough PA, Bisson C, Baker PJ. (Identification and structural analysis of the tripartite alpha-pore forming toxin of Aeromonas hydrophila). Nat Commun. 2019 Jul 1;10(1):2900. doi: 10.1038/s41467-019-10777-x. PMID:31263098 doi:http://dx.doi.org/10.1038/s41467-019-10777-x
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