Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures

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Authors	SABIN Charles MITCHELL Edward P. POKORNÁ Martina GAUTIER Catherine UTILE J. WIMMEROVÁ Michaela IMBERTY Anne
Year of publication	2006
Type	Article in Periodical
Magazine / Source	FEBS Letters
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	Pseudomonas aeruginosa; lectin; cystic fibrosis
Description	The PA-IIL lectin from Pseudomonas aeruginosa is involved in host recognition and biofilm formation. The lectin displays an unusually high affinity for fucose but also binds to L-fucose, L-galactose and D-arabinose that differ only by the group at position 5 of the sugar ring. ITC experiments provided precise determination of affinity for the three methyl-glycosides and revealed a large enthalpy contribution. The crystal structures of the complexes of PA-IIL with L-galactose and Met-â-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. Combination of structures and thermodynamics provided clues for the role of the hydrophobic group in affinity.
Related projects:	Proteins in metabolism and interaction of organisms with the environment