3o44

Crystal Structure of the Vibrio cholerae Cytolysin (HlyA) Heptameric Pore

spinqualitylabelsall models 3o44, resolution 2.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o44 is a 14 chain structure with sequence from Vibrio cholerae 12129(1). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1xez Gene: VCG_000884 (Vibrio cholerae 12129(1)) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemolysin 3D structures

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