Open AccessN‐terminal truncation enables crystallization of the receptor‐binding domain of the FedF bacterial adhesin
Author(s) -
De Kerpel Maia,
Van Molle Inge,
Brys Lea,
Wyns Lode,
De Greve Henri,
Bouckaert Julie
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106049281
Subject(s) - fimbria , bacterial adhesin , glycoconjugate , receptor , escherichia coli , biology , enterotoxigenic escherichia coli , microbiology and biotechnology , glycan , egf like domain , binding domain , chemistry , biochemistry , binding site , glycoprotein , enterotoxin , gene
FedF is the two‐domain tip adhesin of F18 fimbriae from enterotoxigenic Escherichia coli . Bacterial adherence, mediated by the N‐terminal receptor‐binding domain of FedF to carbohydrate receptors on intestinal microvilli, causes diarrhoea and oedema disease in newly weaned piglets and induces the secretion of Shiga toxins. A truncate containing only the receptor‐binding domain of FedF was found to be further cleaved at its N‐terminus. Reconstruction of this N‐terminal truncate rendered FedF amenable to crystallization, resulting in crystals with space group P 2 1 2 1 2 1 and unit‐cell parameters a = 36.20, b = 74.64, c = 99.03 Å that diffracted to beyond 2 Å resolution. The binding specificity of FedF was screened for on a glycan array, exposing 264 glycoconjugates, to identify specific receptors for cocrystallization with FedF.