6r1j

Structure of the soluble AhlC triple head mutant of the tripartite alpha-pore forming toxin, AHL, from Aeromonas hydrophila.

spinqualitylabelsall models 6r1j, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r1j is a 2 chain structure with sequence from Aeromonas hydrophila J-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.92Å Ligands: NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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