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FEBS Lett. 2003 Dec 4;555(2):297-301.

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

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CERMAV-CNRS (affiliated with Université Joseph Fourier), PO Box 53, F-38041 Grenoble Cedex 09, France.


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.

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