3zw2 | pdb_00003zw2

Structure of the lectine Bambl from Burkholderia ambifaria in complex with blood group H type 1 tetrasaccharide

spinqualitylabelsall models 3zw2, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zw2 is a 3 chain structure with sequence from Burkholderia ambifaria. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FUC, GAL, GLA, NAG Related: 3zw1, 3zw0, 3zwe, 3zzv Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Burkholderia ambifaria is generally associated with the rhizosphere of plants where it has biocontrol effects on other microorganisms. It is also a member of the Burkholderia cepacia complex, a group of closely related bacteria that cause lung infections in immunocompromised patients as well as in patients with granulomatous disease or cystic fibrosis. Our previous work indicated that fucose on human epithelia is a frequent target for lectins and adhesins of lung pathogens (Sulak, O., Cioci, G., Lameignere, E., Balloy, V., Round, A., Gutsche, I., Malinovska, L., Chignard, M., Kosma, P., Aubert, D. F., Marolda, C. L., Valvano, M. A., Wimmerova, M., and Imberty, A. (2011) PLoS Pathog. 7, e1002238). Analysis of the B. ambifaria genome identified BambL as a putative fucose-binding lectin. The 87-amino acid protein was produced recombinantly and demonstrated to bind to fucosylated oligosaccharides with a preference for alphaFuc1-2Gal epitopes. Crystal structures revealed that it associates as a trimer with two fucose-binding sites per monomer. The overall fold is a six-bladed beta-propeller formed by oligomerization as in the Ralstonia solanacearum lectin and not by sequential domains like the fungal fucose lectin from Aleuria aurantia. The affinity of BambL for small fucosylated glycans is very high as demonstrated by microcalorimetry (K(D) < 1 mum). Plant cell wall oligosaccharides and human histo-blood group oligosaccharides H-type 2 and Lewis Y are bound with equivalent efficiency. Binding to artificial glycosphingolipid-containing vesicles, human saliva, and lung tissues confirmed that BambL could recognize a wide spectrum of fucosylated epitopes, albeit with a lower affinity for biological material from nonsecretor individuals. Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes.,Audfray A, Claudinon J, Abounit S, Ruvoen-Clouet N, Larson G, Smith DF, Wimmerova M, Le Pendu J, Romer W, Varrot A, Imberty A J Biol Chem. 2012 Feb 3;287(6):4335-47. Epub 2011 Dec 14. PMID:22170069 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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