4aoc

crystal structure of BC2L-A Lectin from Burkolderia cenocepacia in complex with methyl-heptoside

spinqualitylabelsall models 4aoc, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aoc is a 5 chain structure with sequence from Burca. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A1Q, CA, SO4 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Bacteria from the Burkholderia cepacia complex (Bcc) cause highly contagious pneumonia among cystic fibrosis (CF) patients. Among them, Burkholderia cenocepacia is one of the most dangerous in the Bcc and is the most frequent cause of morbidity and mortality in CF patients. Indeed, it is responsible of "cepacia syndrome", a deadly exacerbation of infection, that is the main cause of poor outcomes in lung transplantation. B. cenocepacia produces several soluble lectins with specificity for fucosylated and mannosylated glycoconjugates. These lectins are present on the bacterial cell surface and it has been proposed that they bind to lipopolysaccharide epitopes. In this work, we report on the interaction of one B. cenocepacia lectin, BC2L-A, with heptose and other manno configured sugar residues. Saturation Transfer Difference (STD) NMR spectroscopy studies of BC2L-A with different mono- and disaccharides demonstrated the requirement of manno configuration with hydroxyl or glycol group at C6 for the binding process. The crystal structure of BC2L-A complexed with the methyl-heptoside confirmed the location of the carbohydrate ring in the binding site and elucidated the orientation of the glycol tail, in agreement with NMR data. Titration calorimetry performed on monosaccharides, heptose disaccharides and bacterial heptose-containing oligosaccharides and polysaccharides confirmed that bacterial cell wall contains carbohydrate epitopes that can bind to BC2L-A. Additionally, the specific binding of fluorescent BC2L-A lectin on B. cenocepacia bacterial surface was demonstrated by electron microscopy. Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide.,Marchetti R, Malinovska L, Lameignere E, Adamova L, de Castro C, Cioci G, Stanetty C, Kosma P, Molinaro A, Wimmerova M, Imberty A, Silipo A Glycobiology. 2012 Jul 3. PMID:22763039 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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