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Structural basis of calcium and galactose recognition by the lectin PA‐IL of Pseudomonas aeruginosa
Author(s) -
Cioci Gianluca,
Mitchell Edward P,
Gautier Catherine,
Wimmerová Michaela,
Sudakevitz Dvora,
Pérez Serge,
Gilboa-Garber Nechama,
Imberty Anne
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01249-3
Subject(s) - galactose , lectin , chemistry , calcium , ligand (biochemistry) , hydrogen bond , pseudomonas aeruginosa , biochemistry , monomer , stereochemistry , molecule , receptor , biology , organic chemistry , bacteria , genetics , polymer
The structure of the tetrameric Pseudomonas aeruginosa lectin I (PA‐IL) in complex with galactose and calcium was determined at 1.6 Å resolution, and the native protein was solved at 2.4 Å resolution. Each monomer adopts a β‐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.