N-terminal Truncation Enables Crystallization of the Receptor-binding Domain of the FedF Bacterial Adhesin

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2006 Dec 5

PMID 17142917

Citations 6

Authors

Maia De Kerpel

Inge Van Molle

Lea Brys

Lode Wyns

Henri De Greve

Julie Bouckaert

Affiliations

Soon will be listed here.

Abstract

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 P2(1)2(1)2(1) and unit-cell parameters a = 36.20, b = 74.64, c = 99.03 A that diffracted to beyond 2 A resolution. The binding specificity of FedF was screened for on a glycan array, exposing 264 glycoconjugates, to identify specific receptors for cocrystallization with FedF.

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