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

2006; Wiley; Volume: 580; Issue: 3 Linguagem: Inglês

10.1016/j.febslet.2006.01.030

1873-3468

Charles Sabin, Edward P. Mitchell, Martina Pokorná, Catherine Gautier, Jean‐Pierre Utille, Michaela Wimmerová, Anne Imberty,

Lipid Membrane Structure and Behavior

The lectin from Pseudomonas aeruginosa (PA-IIL) is involved in host recognition and biofilm formation. Lectin not only 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. Isothermal calorimetry 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-beta-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. A combination of the structures and thermodynamics provided clues for the role of the hydrophobic group in affinity.