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

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 calo...

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Veröffentlicht in:FEBS letters 2006-02, Vol.580 (3), p.982-987
Hauptverfasser: Sabin, Charles, Mitchell, Edward P., Pokorná, Martina, Gautier, Catherine, Utille, Jean-Pierre, Wimmerová, Michaela, Imberty, Anne
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container_end_page 987
container_issue 3
container_start_page 982
container_title FEBS letters
container_volume 580
creator Sabin, Charles
Mitchell, Edward P.
Pokorná, Martina
Gautier, Catherine
Utille, Jean-Pierre
Wimmerová, Michaela
Imberty, Anne
description 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.
doi_str_mv 10.1016/j.febslet.2006.01.030
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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. 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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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>16438968</pmid><doi>10.1016/j.febslet.2006.01.030</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record>
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subjects Adhesins, Bacterial - chemistry
Adhesins, Bacterial - metabolism
Ara
Arabinose
Binding Sites - physiology
Biofilms - growth & development
Crystal structure
Cystic fibrosis
d-arabinose
d-mannose
Fuc
Galactose
l-fucose
l-Gal
l-galactose
Lectin
lectin II from Pseudomonas aeruginosa
Lectins - chemistry
Lectins - metabolism
Man
Me-α-Fuc
Me-α-l-Gal
Me-α-Man
Me-β-Ara
Monosaccharides - chemistry
Monosaccharides - metabolism
PA-IIL
Protein Binding - physiology
Protein Structure, Tertiary
Pseudomonas aeruginosa
Pseudomonas aeruginosa - chemistry
Pseudomonas aeruginosa - physiology
Thermodynamics
α-methyl-d-mannopyranoside
α-methyl-l-fucopyranoside
α-methyl-l-galactopyranoside
β-methyl-d-arabinopyranoside
title Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures
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