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Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin
Publication Type:
Journal ArticleSource:
Acta Crystallogr. D, Volume 59, Issue Pt 6, p.1012 - 1015 (2003)URL:
PM:12777763Keywords:
Acetylglucosamine; chemistry; Adhesins; Bacterial; Carrier Proteins; metabolism; Crystallization; Escherichia coli Proteins; Hydrogen Bonding; Indicators and Reagents; Ligands; Models; Molecular; Protein Binding; Receptors; Cell Surface; Selenium CompoundsAbstract:
The Escherichia coli adhesin F17-G is a carbohydrate-binding protein that allows the bacterium to attach to the intestinal epithelium of young ruminants. The structure of the 17 kDa lectin domain of F17-G was determined using the anomalous dispersion signal of a selenium-containing analogue of the monosaccharide ligand N-acetyl-d-glucosamine in which the anomeric oxygen was replaced by an Se atom. A three-wavelength MAD data set yielded good experimental phases to 2.6 A resolution. The structure was refined to 1.75 A resolution and was used to solve the structures of the ligand-free protein and the F17-G-N-acetyl-d-glucosamine complex. This selenium-carbohydrate phasing method could be of general use for determining the structures of carbohydrate-binding proteins
Notes:
DA - 20030602
IS - 0907-4449 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Adhesins, Bacterial)
RN - 0 (Carrier Proteins)
RN - 0 (Escherichia coli Proteins)
RN - 0 (F17-G adhesin protein, E coli)
RN - 0 (Indicators and Reagents)
RN - 0 (Ligands)
RN - 0 (Receptors, Cell Surface)
RN - 0 (Selenium Compounds)
RN - 0 (saccharide-binding proteins)
RN - 7512-17-6 (Acetylglucosamine)
SB - IM