Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures
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- 作者：Charles Sabin ; Edward P. Mitchell ; Martina Pokorná ; Catherine Gautier ; Jean-Pierre Utille ; Michaela Wimmerová ; and Anne Imberty
- 关键词：Lectin ; Cystic fibrosis ; Crystal structure ; Thermodynamics ; Galactose ; Arabinose ; Pseudomonas aeruginosa
- 刊名：FEBS Letters
- 出版年：2006
- 出版时间：6 February 2006
- 年：2006
- 卷：580
- 期：3
- 页码：982-987
- 全文大小：368 K
文摘
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.