Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity
Figure 4
Crystal structure of apoBC2L-C C-terminal domain.
A. Dimeric organisation of apo-BC2L-C-Ct, the protein is represented as ribbon. The sulphate ion close to one of the calcium and monosaccharide binding site is represented as sticks. B. Open conformation of the binding site in the absence of calcium and ligand. The sulphate ion interacts with Gln204, His177 and water molecules. C. Molecular modelling of BC2L-C-Ct in complex with calcium and α-methyl-mannoside with rearrangement of binding amino acids. D. Model of the complex with α-methyl-heptoside.