TY - JOUR
T1 - Crystallization of the B chain of Shiga-like toxin I from Escherichia coli
AU - Hart, P. John
AU - Monzingo, Arthur F.
AU - Donohue-Rolfe, Arthur
AU - Keusch, Gerald T.
AU - Calderwood, Stephen B.
AU - Robertus, Jon D.
N1 - Funding Information:
We are grateful to Dr Stephen Ernst for helpful discussions, to Anne Kane for help in purifying the B subunit, and to Raquelle Smalley for her help in preparing the Figures. This work was supported by grants GM30048 and GM35989 from the National Institute of Health and by a grant from the Foundation for Research (to J.D.R.), and by NIH grants AI20325 (A.D.R.), AI16242 (G.T.K.), AI27239 (S.B.C.) and by grant A&I34928 to the Center for Gastroenterology Research from NIADDKD.
Copyright:
Copyright 2015 Elsevier B.V., All rights reserved.
PY - 1991/4/20
Y1 - 1991/4/20
N2 - 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 ammo 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 P212121, 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.
AB - 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 ammo 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 P212121, 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.
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U2 - 10.1016/0022-2836(91)90256-6
DO - 10.1016/0022-2836(91)90256-6
M3 - Article
C2 - 2023244
AN - SCOPUS:0025783017
VL - 218
SP - 691
EP - 694
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -