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

被引:86
|
作者
Sabin, C
Mitchell, EP
Pokorná, M
Gautier, C
Utille, JP
Wimmerová, M
Imberty, A
机构
[1] Univ Grenoble 1, CNRS, CERMAV, F-38041 Grenoble 09, France
[2] ESRF, Expt Div, F-38043 Grenoble 09, France
[3] Masaryk Univ, Natl Ctr Biomol Res, CS-61137 Brno, Czech Republic
[4] Masaryk Univ, Dept Biochem, CS-61137 Brno, Czech Republic
关键词
lectin; cystic fibrosis; crystal structure; thermodynamics; galactose; Arabinose; Pseudomonas aeruginosa;
D O I
10.1016/j.febslet.2006.01.030
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:982 / 987
页数:6
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