1o9v
From Proteopedia
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F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE
Overview
The F17-G adhesin at the tip of flexible F17 fimbriae of enterotoxigenic, Escherichia coli mediates binding to, N-acetyl-beta-D-glucosamine-presenting receptors on the microvilli of the, intestinal epithelium of ruminants. We report the 1.7 A resolution crystal, structure of the lectin domain of F17-G, both free and in complex with, N-acetylglucosamine. The monosaccharide is bound on the side of the, ellipsoid-shaped protein in a conserved site around which all natural, variations of F17-G are clustered. A model is proposed for the interaction, between F17-fimbriated E. coli and microvilli with enhanced affinity, compared with the binding constant we determined for F17-G binding to, N-acetylglucosamine (0.85 mM-1). Unexpectedly, the F17-G structure reveals, that the lectin domains of the ... [(full description)]
About this Structure
1O9V is a [Single protein] structure of sequence from [Escherichia coli] with SNG as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine., Buts L, Bouckaert J, De Genst E, Loris R, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H, Mol Microbiol. 2003 Aug;49(3):705-15. PMID:12864853
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