1O9W

F17-aG lectin domain from Escherichia coli in complex with N-acetyl-glucosamine

1O9W の概要

• エントリーDOI: 10.2210/pdb1o9w/pdb
• 関連するPDBエントリー: 1O9V 1O9Z
• 分子名称: F17A-G FIMBRIAL ADHESIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: bacterial adhesin, bacterial attachment, sugar binding protein pathogenesis, immunoglobulin fold, sugar binding protein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19269.43

構造登録者

Buts, L.,De Genst, E.,Loris, R.,Oscarson, S.,Lahmann, M.,Messens, J.,Brosens, E.,Wyns, L.,Bouckaert, J.,De Greve, H. (登録日: 2002-12-20, 公開日: 2003-05-29, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.65 Å)