title: Crystallization of the B chain of Shiga-like toxin I from Escherichia coli.
abstract: Shiga-like toxin I (SLT-I) is produced by several pathogenic strains of Escherichia coli associated with diarrheal disease. The toxin consists of an A chain, which attacks eukaryotic ribosomes, inhibiting protein synthesis, and multiple copies of a 69 amino acid B chain. The B subunit mediates cell binding and uptake through its interactions with cell surface carbohydrate moieties. Here we report that the B chain has been crystallized in a form suitable for high-resolution X-ray analysis. The space group is P2(1)2(1)2(1), with a = 56.2 A, b = 59.9 A and c = 102.5 A. A rotation function using three-dimensional diffraction data suggests that the asymmetric unit is a tetramer.
authors.affiliation: Clayton Foundation Biochemical Institute, Department of Chemistry and Biochemistry, University of Texas, Austin 78712.
authors.forename: P J
authors.initials: PJ
authors.lastname: Hart
authors.forename: A F
authors.initials: AF
authors.lastname: Monzingo
authors.forename: A
authors.initials: A
authors.lastname: Donohue-Rolfe
authors.forename: G T
authors.initials: GT
authors.lastname: Keusch
authors.forename: S B
authors.initials: SB
authors.lastname: Calderwood
authors.forename: J D
authors.initials: JD
authors.lastname: Robertus
mesh_terms: D001427:Bacterial Toxins / Q000737:chemistry*; D004926:Escherichia coli / Q000032:analysis*; D011487:Protein Conformation; D022622:Shiga Toxin 1; D014961:X-Ray Diffraction
chemical_list: D001427:Bacterial Toxins; D022622:Shiga Toxin 1