Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa:: Thermodynamics data correlated with X-ray structures
Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa:: Thermodynamics data correlated with X-ray structures
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DOI：
10.1016/j.febslet.2006.01.030
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发表时间：
2006-02-06
期刊：
影响因子：
3.5
通讯作者：
Imberty, A
中科院分区：
文献类型：
--
作者：
Sabin, C;Mitchell, EP;Imberty, A
铜绿假单胞菌凝集素(PA-IIL)参与宿主识别和生物被膜的形成。凝集素不仅对岩藻糖表现出异常高的亲和力，而且还与L-岩藻糖、L-半乳糖和D-阿拉伯糖结合，这三种糖只是糖环5位上的基团不同。等温量热实验精确地测定了三种甲基糖苷的亲和力，并揭示了较大的热焓贡献。测定了PA-IIL与L-半乳糖和甲硫氨酸-β-D-阿拉伯糖苷的配合物的晶体结构，并与前述的PA-IIL/岩藻糖配合物进行了比较。结构和热力学的结合为疏水基团在亲和力中的作用提供了线索。(C)2006年欧洲生化学会联合会。爱思唯尔出版，版权所有。
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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.