Publication details
Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: Thermodynamics data correlated with X-ray structures
| Authors | |
|---|---|
| Year of publication | 2006 |
| Type | Article in Periodical |
| Magazine / Source | FEBS Letters |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Pseudomonas aeruginosa; lectin; cystic fibrosis |
| Description | The PA-IIL lectin from Pseudomonas aeruginosa is involved in host recognition and biofilm formation. The lectin 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. ITC 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-â-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. Combination of structures and thermodynamics provided clues for the role of the hydrophobic group in affinity. |
| Related projects: |