Structural basis of calcium and galactose recognition by the lectin PA IL of Pseudomonas aeruginosa

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Authors	CIOCCI Gianluca MITCHELL Edward GAUIER Catherine WIMMEROVÁ Michaela SUDAKEVITZ Dvora PÉREZ Serge GILBOA-GARBER Nechama IMBERTY Anne
Year of publication	2003
Type	Article in Periodical
Magazine / Source	FEBS Letters
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	pseudomonas aeruginosa; cystic fibrosis; lectin; crystal structure
Description	The structure of the tetrameric Pseudomonas aeruginosa lectin I (PA-IL) in complex with galactose and calcium was determined at 1.6 A esolution, 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 coordination of the calcium ion. The stereochemistry of calcium galactose binding is reminiscent to that observed in some animal C-type lectins. The structure of the complex provides a framework for future design of anti-bacterial compounds.
Related projects:	Biomolecular Structure-function Relationships and their role in the Metabolism