Crystallization of the B chain of Shiga-like toxin I from Escherichia coli

P. John Hart, Arthur F. Monzingo, Arthur Donohue-Rolfe, Gerald T. Keusch, Stephen B. Calderwood, Jon D. Robertus

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

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 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.

Original languageEnglish (US)
Pages (from-to)691-694
Number of pages4
JournalJournal of Molecular Biology
Volume218
Issue number4
DOIs
StatePublished - Apr 20 1991

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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