Structural highlights
Function
PA1L_PSEAE D-galactose specific lectin. Binds in decreasing order of affinity: melibiose, methyl-alpha-D-galactoside, D-galactose, methyl-beta-D-galactoside, N-acetyl-D-galactosamine. Similar to plant lectins in its selective (carbohydrate-specific) hemagglutinating activity.
Publication Abstract from PubMed
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.
Structural basis of calcium and galactose recognition by the lectin PA-IL of Pseudomonas aeruginosa.,Cioci G, Mitchell EP, Gautier C, Wimmerova M, Sudakevitz D, Perez S, Gilboa-Garber N, Imberty A FEBS Lett. 2003 Dec 4;555(2):297-301. PMID:14644431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cioci G, Mitchell EP, Gautier C, Wimmerova M, Sudakevitz D, Perez S, Gilboa-Garber N, Imberty A. Structural basis of calcium and galactose recognition by the lectin PA-IL of Pseudomonas aeruginosa. FEBS Lett. 2003 Dec 4;555(2):297-301. PMID:14644431
