Structural highlights
Function
Q9HYN5_PSEAE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: thermodynamics data correlated with X-ray structures.,Sabin C, Mitchell EP, Pokorna M, Gautier C, Utille JP, Wimmerova M, Imberty A FEBS Lett. 2006 Feb 6;580(3):982-7. Epub 2006 Jan 19. PMID:16438968[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sabin C, Mitchell EP, Pokorna M, Gautier C, Utille JP, Wimmerova M, Imberty A. Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: thermodynamics data correlated with X-ray structures. FEBS Lett. 2006 Feb 6;580(3):982-7. Epub 2006 Jan 19. PMID:16438968 doi:http://dx.doi.org/10.1016/j.febslet.2006.01.030
