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N-terminal truncation enables crystallization of the receptor-binding domain of the FedF bacterial adhesin
Publication Type:
Journal ArticleSource:
Acta Cryst. F, Volume 62, Issue Pt 12, p.1278 - 1282 (2006)URL:
PM:17142917Keywords:
Adhesins; Bacterial; chemistry; Amino Acid Sequence; Cloning; Molecular; Crystallization; Crystallography; X-Ray; Escherichia coli Proteins; Molecular Sequence Data; Peptide Fragments; Protein Structure; Tertiary; Receptors; Immunologic; metabolism; Sequence AAbstract:
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
Notes:
DA - 20061204 IS - 1744-3091 (Electronic) LA - eng PT - Journal Article PT - Research Support, N.I.H., Extramural PT - Research Support, Non-U.S. Gov't RN - 0 (Adhesins, Bacterial) RN - 0 (Escherichia coli Proteins) RN - 0 (FedF protein, E coli) RN - 0 (Peptide Fragments) RN - 0 (Receptors, Immunologic) RN - 0 (bacterial adhesin receptor) SB - IM