2vuc | pdb_00002vuc

PA-IIL LECTIN FROM PSEUDOMONAS AERUGINOSA COMPLEXED WITH FUCOSE-DERIVED GLYCOMIMETICS

spinqualitylabelsall models 2vuc, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vuc is a 4 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FUC, SO4, YX0 Related: 1ovs, 1oxc, 1w8f, 2jdk, 1oux, 1gzt, 2jdh, 2jdy, 1ous, 2jdu, 1ovp, 2jdp, 1our, 1uzv, 2boj, 2bp6, 2jdm, 2jdn, 1w43, 1w8h, 2vud Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients.,Mitchell E, Houles C, Sudakevitz D, Wimmerova M, Gautier C, Perez S, Wu AM, Gilboa-Garber N, Imberty A Nat Struct Biol. 2002 Dec;9(12):918-21. PMID:12415289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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