This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1oio
From Proteopedia
|
GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI
Overview
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 ... [(full description)]
About this Structure
1OIO is a [Single protein] structure of sequence from [Escherichia coli] with NAG as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 15:55:31 2007
