Structural basis of calcium and galactose recognition by the lectin PA-IL of Pseudomonas aeruginosa.
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.
Cioci
Gianluca
G
CERMAV-CNRS (affiliated with Université Joseph Fourier), PO Box 53, F-38041 Grenoble Cedex 09, France.
Mitchell
Edward P
EP
Gautier
Catherine
C
Wimmerová
Michaela
M
Sudakevitz
Dvora
D
Pérez
Serge
S
Gilboa-Garber
Nechama
N
Imberty
Anne
A
D018829:Adhesins, Bacterial / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D005690:Galactose / Q000737:chemistry / Q000378:metabolism*; D006860:Hydrogen Bonding; D037102:Lectins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000378:metabolism*
D018829:Adhesins, Bacterial; D037102:Lectins; C038692:adhesin, Pseudomonas; D002118:Calcium; D005690:Galactose