3o44

<StructureSection load='3o44' size='340' side='right' caption='[[3o44]], [[Resolution|resolution]] 2.88&Aring;' scene=''>

<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>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xez|1xez]]</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'>[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://www.rcsb.org/pdb/explore.do?structureId=3o44 RCSB], [http://www.ebi.ac.uk/pdbsum/3o44 PDBsum]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

 

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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*[[Hemolysin|Hemolysin]]

[[Category: De, S]]

[[Category: Olson, R]]

[[Category: Beta-barrel]]

[[Category: Toxin]]