Title | 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 Article |
Year of Publication | 2003 |
Authors | Buts, L., R. Loris, E. De Genst, S. Oscarson, M. Lahmann, J. Messens, E. Brosens, L. Wyns, H. De Greve, and J. Bouckaert |
Journal | Acta Crystallogr D Biol Crystallogr |
Volume | 59 |
Issue | Pt 6 |
Pagination | 1012-5 |
Date Published | 2003 Jun |
ISSN | 0907-4449 |
Keywords | Acetylglucosamine, Adhesins, Bacterial, Carrier Proteins, Crystallization, Escherichia coli Proteins, Hydrogen Bonding, Indicators and Reagents, Ligands, Models, Molecular, Protein Binding, Receptors, Cell Surface, Selenium Compounds |
Abstract | 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. |
Alternate Journal | Acta Crystallogr. D Biol. Crystallogr. |
PubMed ID | 12777763 |
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