3g4n

Crystal structure of the activated aerolysin mutant H132D

spinqualitylabelsall models 3g4n, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3g4n is a 2 chain structure with sequence from "aeromonas_liquefaciens"_kluyver_and_van_niel_1936 "aeromonas liquefaciens" kluyver and van niel 1936. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1pre, 3c0n, 3g4o, 1z52 Gene: aerA ("Aeromonas liquefaciens" Kluyver and van Niel 1936) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AERA_AERHY] Aerolysin is a cytolytic toxin exported by the Gram negative Aeromonas bacteria. The mature toxin binds to eukaryotic cells and aggregates to form holes approximately 3 nm in diameter, leading to destruction of the membrane permeability barrier and osmotic lysis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Throughout evolution, one of the most ancient forms of aggression between cells or organisms has been the production of proteins or peptides affecting the permeability of the target cell membrane. This class of virulence factors includes the largest family of bacterial toxins, the pore-forming toxins (PFTs). PFTs are bistable structures that can exist in a soluble and a transmembrane state. It is unclear what drives biosynthetic folding towards the soluble state, a requirement that is essential to protect the PFT-producing cell. Here we have investigated the folding of aerolysin, produced by the human pathogen Aeromonas hydrophila, and more specifically the role of the C-terminal propeptide (CTP). By combining the predictive power of computational techniques with experimental validation using both structural and functional approaches, we show that the CTP prevents aggregation during biosynthetic folding. We identified specific residues that mediate binding of the CTP to the toxin. We show that the CTP is crucial for the control of the aerolysin activity, since it protects individual subunits from aggregation within the bacterium and later controls assembly of the quaternary pore-forming complex at the surface of the target host cell. The CTP is the first example of a C-terminal chain-linked chaperone with dual function. Dual chaperone role of the C-terminal propeptide in folding and oligomerization of the pore-forming toxin aerolysin.,Iacovache I, Degiacomi MT, Pernot L, Ho S, Schiltz M, Dal Peraro M, van der Goot FG PLoS Pathog. 2011 Jul;7(7):e1002135. Epub 2011 Jul 14. PMID:21779171 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aerolysin

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