QuickView for alpha- toxin (biogroup)

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Description:: The following small plant proteins are evolutionary related:Gamma-thionins from Triticum aestivum (Wheat) endosperm (gamma-purothionins) and gamma-hordothionins from Hordeum vulgare(Barley) are toxic to animal cells and inhibit protein synthesis in cell free systems.A flower-specific thionin (FST) from Nicotiana tabacum (Common Tobacco).Antifungal proteins (AFP) from the seeds of Brassicaceae species such as radish, mustard, turnip and Arabidopsis thaliana (Thale Cress).Inhibitors of insect alpha-amylases from sorghum.Probable protease inhibitor P322 from Solanum tuberosum (Potato).A germination-related protein from Vigna unguiculata (Cowpea).Anther-specific protein SF18 from sunflower. SF18 is a protein that contains a gamma-thionin domain at its N terminus and a proline-rich C-terminal domain.Glycine max (Soybean) sulphur-rich protein SE60.Vicia faba (Broad bean) antibacterial peptides fabatin-1 and -2.In their mature form, these proteins generally consist of about 45 to 50 amino-acid residues. As shown in the following schematic representation, these peptides contain eight conserved cysteines involved in disulphide bonds. +-------------------------------------------+ | +-------------------+ | | | | | xxCxxxxxxxxxxCxxxxxCxxxCxxxxxxxxxCxxxxxxCxCxxxC | | | | +---|----------------+ | +------------------+'C': conserved cysteine involved in a disulphide bond.The folded structure of Gamma-purothionin is characterised by a well-defined 3-stranded anti-parallel beta-sheet and a short alpha-helix. Three disulphide bridges are located in the hydrophobic core between the helix and sheet, forming a cysteine-stabilised alpha-helical motif. This structure differs from that of the plant alpha- and beta- thionins, but is analogous to scorpion toxins and insect defensins.

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