1O9Z

F17-aG lectin domain from Escherichia coli (ligand free)

Summary for 1O9Z

• Entry DOI: 10.2210/pdb1o9z/pdb
• Related: 1O9V 1O9W
• Descriptor: F17-AG LECTIN DOMAIN (2 entities in total)
• Functional Keywords: bacterial adhesin, lectin, bacterial attachment, pathogenesis, immunoglobulin fold
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 19064.23

Authors

Buts, L.,De Genst, E.,Loris, R.,Oscarson, S.,Lahmann, M.,Messens, J.,Brosens, E.,Wyns, L.,Bouckaert, J.,De Greve, H. (deposition date: 2002-12-23, release date: 2003-05-29, Last modification date: 2023-12-13)

Primary citation

Buts, L.,Bouckaert, J.,De Genst, E.,Loris, R.,Oscarson, S.,Lahmann, M.,Messens, J.,Brosens, E.,Wyns, L.,De Greve, H.
The Fimbrial Adhesin F17-G of Enterotoxigenic Escherichia Coli Has an Immunoglobulin-Like Lectin Domain that Binds N-Acetylglucosamine
Mol.Microbiol., 49:705-, 2003

PubMed Abstract: 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.

PubMed: 12864853
DOI: 10.1046/J.1365-2958.2003.03600.X

Experimental method

X-RAY DIFFRACTION (1.75 Å)