1OIO

GafD (F17c-type) Fimbrial adhesin from Escherichia coli

1OIO の概要

• エントリーDOI: 10.2210/pdb1oio/pdb
• 分子名称: FIMBRIAL LECTIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: lectin, adhesin, n-acetyl-d-glucosamine binding, glcnac binding lectin
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Fimbrium (By similarity): Q47341
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39054.94

構造登録者

Merckel, M.C.,Tanskanen, J.,Edelman, S.,Westerlund-Wikstrom, B.,Korhonen, T.K.,Goldman, A. (登録日: 2003-06-22, 公開日: 2003-08-15, 最終更新日: 2024-11-06)

主引用文献

Merckel, M.C.,Tanskanen, J.,Edelman, S.,Westerlund-Wikstrom, B.,Korhonen, T.K.,Goldman, A.
The Structural Basis of Receptor-Binding by Escherichia Coli Associated with Diarrhea and Septicemia
J.Mol.Biol., 331:897-, 2003

PubMed Abstract: GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal disease, and the structure of the ligand-binding domain, GafD1-178, has been determined at 1.7A resolution in the presence of the receptor sugar N-acetyl-D-glucosamine. The overall fold is a beta-barrel jelly-roll fold. The ligand-binding site was identified and localized to the side of the molecule. Receptor binding is mediated by side-chain as well main-chain interactions. Ala43-Asn44, Ser116-Thr117 form the sugar acetamide specificity pocket, while Asp88 confers tight binding and Trp109 appears to position the ligand. There is a disulfide bond that rigidifies the acetamide specificity pocket. The three fimbrial lectins, GafD, FimH and PapG share similar beta-barrel folds but display different ligand-binding regions and disulfide-bond patterns. We suggest an evolutionary path for the evolution of the very diverse fimbrial lectins from a common ancestral fold.

PubMed: 12909017
DOI: 10.1016/S0022-2836(03)00841-6

実験手法

X-RAY DIFFRACTION (1.7 Å)