1uwf

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spinqualitylabelsall models 1uwf, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

1.7 A RESOLUTION STRUCTURE OF THE RECEPTOR BINDING DOMAIN OF THE FIMH ADHESIN FROM UROPATHOGENIC E. COLI

Overview

Mannose-binding type 1 pili are important virulence factors for the, establishment of Escherichia coli urinary tract infections (UTIs). These, infections are initiated by adhesion of uropathogenic E. coli to uroplakin, receptors in the uroepithelium via the FimH adhesin located at the tips of, type 1 pili. Blocking of bacterial adhesion is able to prevent infection., Here, we provide for the first time binding data of the molecular events, underlying type 1 fimbrial adherence, by crystallographic analyses of the, FimH receptor binding domains from a uropathogenic and a K-12 strain, and, affinity measurements with mannose, common mono- and disaccharides, and a, series of alkyl and aryl mannosides. Our results illustrate that the, lectin domain of the FimH adhesin is a stable and functional ... [(full description)]

About this Structure

1UWF is a [Single protein] structure of sequence from [Escherichia coli] with DEG and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin., Bouckaert J, Berglund J, Schembri M, De Genst E, Cools L, Wuhrer M, Hung CS, Pinkner J, Slattegard R, Zavialov A, Choudhury D, Langermann S, Hultgren SJ, Wyns L, Klemm P, Oscarson S, Knight SD, De Greve H, Mol Microbiol. 2005 Jan;55(2):441-55. PMID:15659162

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