1OIO

GafD (F17c-type) Fimbrial adhesin from Escherichia coli

Summary for 1OIO

• Entry DOI: 10.2210/pdb1oio/pdb
• Descriptor: FIMBRIAL LECTIN, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: lectin, adhesin, n-acetyl-d-glucosamine binding, glcnac binding lectin
• Biological source: ESCHERICHIA COLI
• Cellular location: Fimbrium (By similarity): Q47341
• Total number of polymer chains: 2
• Total formula weight: 39054.94

Authors

Merckel, M.C.,Tanskanen, J.,Edelman, S.,Westerlund-Wikstrom, B.,Korhonen, T.K.,Goldman, A. (deposition date: 2003-06-22, release date: 2003-08-15, Last modification date: 2020-07-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)