Literature DB >> 16438968

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

Charles Sabin1, Edward P Mitchell, Martina Pokorná, Catherine Gautier, Jean-Pierre Utille, Michaela Wimmerová, Anne Imberty.   

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.

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Year:  2006        PMID: 16438968     DOI: 10.1016/j.febslet.2006.01.030

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  23 in total

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10.  Engineering of PA-IIL lectin from Pseudomonas aeruginosa - Unravelling the role of the specificity loop for sugar preference.

Authors:  Jan Adam; Martina Pokorná; Charles Sabin; Edward P Mitchell; Anne Imberty; Michaela Wimmerová
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