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

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 calo...

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Veröffentlicht in:FEBS letters 2006-02, Vol.580 (3), p.982-987
Hauptverfasser: Sabin, Charles, Mitchell, Edward P., Pokorná, Martina, Gautier, Catherine, Utille, Jean-Pierre, Wimmerová, Michaela, Imberty, Anne
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Sprache:eng
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Zusammenfassung: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-β-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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2006.01.030