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

Varování

Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	CIOCCI Gianluca MITCHELL Edward GAUIER Catherine WIMMEROVÁ Michaela SUDAKEVITZ Dvora PÉREZ Serge GILBOA-GARBER Nechama IMBERTY Anne
Rok publikování	2003
Druh	Článek v odborném periodiku
Časopis / Zdroj	FEBS Letters
Fakulta / Pracoviště MU	Přírodovědecká fakulta
Citace
Obor	Biochemie
Klíčová slova	pseudomonas aeruginosa; cystic fibrosis; lectin; crystal structure
Popis	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.
Související projekty:	Strukturně-funkční vztahy biomolekul a jejich role v metabolismu