Crystallization of the B chain of Shiga-like toxin I from Escherichia coli.
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.
Hart
P J
PJ
Clayton Foundation Biochemical Institute, Department of Chemistry and Biochemistry, University of Texas, Austin 78712.
Monzingo
A F
AF
Donohue-Rolfe
A
A
Keusch
G T
GT
Calderwood
S B
SB
Robertus
J D
JD
D001427:Bacterial Toxins / Q000737:chemistry*; D004926:Escherichia coli / Q000032:analysis*; D011487:Protein Conformation; D022622:Shiga Toxin 1; D014961:X-Ray Diffraction
D001427:Bacterial Toxins; D022622:Shiga Toxin 1