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| | ==Crystal Structure of the Vibrio cholerae Cytolysin (HlyA) Heptameric Pore== | | ==Crystal Structure of the Vibrio cholerae Cytolysin (HlyA) Heptameric Pore== |
| - | <StructureSection load='3o44' size='340' side='right' caption='[[3o44]], [[Resolution|resolution]] 2.88Å' scene=''> | + | <StructureSection load='3o44' size='340' side='right'caption='[[3o44]], [[Resolution|resolution]] 2.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3o44]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae_12129(1) Vibrio cholerae 12129(1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O44 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O44 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3o44]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_12129(1) Vibrio cholerae 12129(1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O44 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xez|1xez]]</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]] 2.88Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VCG_000884 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=592313 Vibrio cholerae 12129(1)])</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=3o44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o44 OCA], [https://pdbe.org/3o44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o44 RCSB], [https://www.ebi.ac.uk/pdbsum/3o44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o44 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=3o44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o44 OCA], [http://pdbe.org/3o44 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o44 RCSB], [http://www.ebi.ac.uk/pdbsum/3o44 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o44 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/HLYA_VIBCH HLYA_VIBCH] Bacterial hemolysin that causes cytolysis by forming heptameric pores in target host membranes.<ref>PMID:15978620</ref> |
| - | Pore-forming toxins (PFTs) are potent cytolytic agents secreted by pathogenic bacteria that protect microbes against the cell-mediated immune system (by targeting phagocytic cells), disrupt epithelial barriers, and liberate materials necessary to sustain growth and colonization. Produced by gram-positive and gram-negative bacteria alike, PFTs are released as water-soluble monomeric or dimeric species, bind specifically to target membranes, and assemble transmembrane channels leading to cell damage and/or lysis. Structural and biophysical analyses of individual steps in the assembly pathway are essential to fully understanding the dynamic process of channel formation. To work toward this goal, we solved by X-ray diffraction the 2.9-A structure of the 450-kDa heptameric Vibrio cholerae cytolysin (VCC) toxin purified and crystallized in the presence of detergent. This structure, together with our previously determined 2.3-A structure of the VCC water-soluble monomer, reveals in detail the architectural changes that occur within the channel region and accessory lectin domains during pore formation including substantial rearrangements of hydrogen-bonding networks in the pore-forming amphipathic loops. Interestingly, a ring of tryptophan residues forms the narrowest constriction in the transmembrane channel reminiscent of the phenylalanine clamp identified in anthrax protective antigen [Krantz BA, et al. (2005) Science 309:777-781]. Our work provides an example of a beta-barrel PFT (beta-PFT) for which soluble and assembled structures are available at high-resolution, providing a template for investigating intermediate steps in assembly.
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| - | Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins.,De S, Olson R Proc Natl Acad Sci U S A. 2011 May 3;108(18):7385-90. Epub 2011 Apr 18. PMID:21502531<ref>PMID:21502531</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3o44" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| - | *[[Hemolysin|Hemolysin]] | + | *[[Hemolysin 3D structures|Hemolysin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: De, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Olson, R]] | + | [[Category: De S]] |
| - | [[Category: Beta-barrel]] | + | [[Category: Olson R]] |
| - | [[Category: Channel]]
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| - | [[Category: Cytolysin]]
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| - | [[Category: Detergent-solubilized]]
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| - | [[Category: Hemolysin]]
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| - | [[Category: Liposome]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Pore-forming toxin]]
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| - | [[Category: Toxin]]
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