1oio
GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI
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OverviewOverview
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.
About this StructureAbout this Structure
1OIO is a Single protein structure of sequence from Escherichia coli with NAG as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia., Merckel MC, Tanskanen J, Edelman S, Westerlund-Wikstrom B, Korhonen TK, Goldman A, J Mol Biol. 2003 Aug 22;331(4):897-905. PMID:12909017
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