|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|
|Date Published||2003 Jun|
|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|
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.|
Solving the phase problem for carbohydrate-binding proteins using selenium derivatives of their ligands: a case study involving the bacterial F17-G adhesin.