Structural Basis of Calcium and Galactose Recognition by the Lectin Pa-Il of Pseudomonas Aeruginosa
Cioci, G., Mitchell, E., Gautier, C., Wimmerova, M., Sudakevitz, D., Perez, S., Gilboa-Garber, N., Imberty, A.(2003) FEBS Lett 555: 297
- PubMed: 14644431 
- DOI: https://doi.org/10.1016/s0014-5793(03)01249-3
- Primary Citation of Related Structures:  
1OKO, 1UOJ - PubMed Abstract: 
The structure of the tetrameric Pseudomonas aeruginosa lectin I (PA-IL) in complex with galactose and calcium was determined at 1.6 A resolution, and the native protein was solved at 2.4 A resolution. Each monomer adopts a beta-sandwich fold with ligand binding site at the apex. All galactose hydroxyl groups, except O1, are involved in a hydrogen bond network with the protein and O3 and O4 also participate in the co-ordination of the calcium ion. The stereochemistry of calcium galactose binding is reminiscent of that observed in some animal C-type lectins. The structure of the complex provides a framework for future design of anti-bacterial compounds.
Organizational Affiliation: 
CERMAV-CNRS (affiliated with Universit¨¦ Joseph Fourier), PO Box 53, F-38041 Grenoble Cedex 09, France.