1o9v

F17-aG lectin domain from Escherichia coli in complex with a selenium carbohydrate derivative

spinqualitylabelsall models 1o9v, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1o9v is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: SNG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F17AG_ECOLX Essential fimbrial adhesion factor that mediates binding to N-acetylglucosamine-containing receptors in the host intestinal microvilli, leading to colonization of the intestinal tissue, and diarrhea or septicemia. Also confers adhesiveness to laminin and basement membranes. Publication Abstract from PubMed 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 F17-G, PapGII and FimH fimbrial adhesins all share the immunoglobulin-like fold of the structural components (pilins) of their fimbriae, despite lack of any sequence identity. Fold comparisons with pilin and chaperone structures of the chaperone/usher pathway highlight the central role of the C-terminal beta-strand G of the immunoglobulin-like fold and provides new insights into pilus assembly, function and adhesion. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adhesin 3D structures

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