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.
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