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1GZT

Pseudomonas aeruginosa lectin II (PA-IIL) together with fucose

Summary for 1GZT
Entry DOI10.2210/pdb1gzt/pdb
DescriptorFUCOSE-SPECIFIC LECTIN, alpha-L-fucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordslectin, sugar-binding protein, fucose
Biological sourcePSEUDOMONAS AERUGINOSA
Total number of polymer chains4
Total formula weight48440.87
Authors
Mitchell, E.,Imberty, A.,Gilboa-Garber, N. (deposition date: 2002-06-06, release date: 2002-11-19, Last modification date: 2024-05-01)
Primary citationMitchell, E.,Houles, C.,Sudakevitz, D.,Wimmerova, M.,Gautier, C.,Perez, S.,Wu, A.M.,Gilboa-Garber, N.,Imberty, A.
Structural Basis for Oligosaccharide-Mediated Adhesion of Pseudomonas Aeruginosa in the Lungs of Cystic Fibrosis Patients
Nat.Struct.Biol., 9:918-, 2002
Cited by
PubMed Abstract: Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Le(a)) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.
PubMed: 12415289
DOI: 10.1038/NSB865
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

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