Binding of Different Monosaccharides by Lectin Pa-iil from Pseudomonas Aeruginosa: Thermodynamics Data Correlated with X-ray Structures.
From: CERMAV-CNRS (affiliated with Université Joseph Fourier), 601 rue de la Chimie, Grenoble BP53, F-38041 Grenoble cedex 09, France.
FEBS letters
- Publish Date: Feb 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 3
- Pages: 982-7
- Medium: Print
- Language: English
- Citation (JAMA): Sabin Charles, Mitchell Edward P, Pokorná Martina, et al. Binding of Different Monosaccharides by Lectin Pa-iil from Pseudomonas Aeruginosa: Thermodynamics Data Correlated with X-ray Structures.. FEBS Lett. Feb 2006;580:982-7
Abstract
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.
Mesh Headings (Keywords): Adhesins, Bacterial, Binding Sites, Biofilms, Lectins, Monosaccharides, Protein Binding, Protein Structure, Tertiary, Pseudomonas aeruginosa, Thermodynamics
Check for Full Text / PubMed Unique Identifier (PMID): 16438968
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