1bos
From Proteopedia
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SHIGA-LIKE TOXIN COMPLEXED WITH ITS RECEPTOR
Overview
Shiga-like toxin I (SLT-I) is a virulence factor of Escherichia coli, strains that cause disease in humans. Like other members of the Shiga, toxin family, it consists of an enzymatic (A) subunit and five copies of a, binding subunit (the B-pentamer). The B-pentamer binds to a specific, glycolipid, globotriaosylceramide (Gb3), on the surface of target cells, and thereby plays a crucial role in the entry of the toxin. Here we, present the crystal structure at 2.8 A resolution of the SLT-I B-pentamer, complexed with an analogue of the Gb3 trisaccharide. The structure reveals, a surprising density of binding sites, with three trisaccharide molecules, bound to each B-subunit monomer of 69 residues. All 15 trisaccharides bind, to one side of the B-pentamer, providing further evidence that this side, faces the cell membrane. The structural model is consistent with data from, site-directed mutagenesis and binding of carbohydrate analogues, and, allows the rational design of therapeutic Gb3 analogues that block the, attachment of toxin to cells.
About this Structure
1BOS is a Single protein structure of sequence from Bacteriophage h30, bacteriophage h19b with GAL as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3., Ling H, Boodhoo A, Hazes B, Cummings MD, Armstrong GD, Brunton JL, Read RJ, Biochemistry. 1998 Feb 17;37(7):1777-88. PMID:9485303
Page seeded by OCA on Tue Nov 20 11:47:58 2007
