Structural and thermodynamical characterisation of interactionbetween a pseudomonas lectin and monosaccharides
2003
Pseudomonas aeruginosa galactose- and fucose-binding (PA-IL and
PA-IIL) lectins contribute to the virulence of this pathogenic
bacterium, which is a major cause of morbidity and mortality in
cystic fibrosis patients. The crystal structure of PA-IIL
complexed with fucose has been solved at 1.3 A and further
refined at 1 Ĺ resolution. Additional experiments have been
performed in order to understand the molecular basis of both
specificity and affinity of PA-IIL for monosaccharides.
Crystals have been obtained for the complex between PA-ILL and
b-Me-D-arabinopyranoside and the structure has been solved at
1.8 A resolution. PA-IIL exhibits unusually high specificity to
fucose, which can be related to the presence of two calcium
ions in the site. Isothermal titration microcalorimetry (ITC)
experiments were performed in order to characterize the
thermodynamic parameters of the interaction since this method
has been proven to be well adapted to the study of
protein/carbohydrate interactions. Several monosaccharides
differing only by the group at C5 (L-fucose, L-galactose and
D-arabinose) were tested, as well as their methyl-glycosides.
Calculations of charges distribution were performed using
quantum chemistry in order to rationalize the role of calcium
ions in the affinity.
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