3ZZV

BambL complexed with Htype2 tetrasaccharide

3ZZV の概要

• エントリーDOI: 10.2210/pdb3zzv/pdb
• 関連するPDBエントリー: 3ZW0 3ZW2 3ZWE
• 関連するBIRD辞書のPRD_ID: PRD_900036
• 分子名称: BAMBL LECTIN, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose, ... (4 entities in total)
• 機能のキーワード: sugar binding protein, cystic fibrosis, beta-propeller, human histo-blood group
• 由来する生物種: BURKHOLDERIA AMBIFARIA
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30973.10

構造登録者

Audfray, A.,Claudinon, J.,Abounit, S.,Ruvoen-Clouet, N.,Larson, G.,Wimmerova, M.,LePendu, J.,Romer, W.,Varrot, A.,Imberty, A. (登録日: 2011-09-05, 公開日: 2011-12-21, 最終更新日: 2023-12-20)

主引用文献

Audfray, A.,Claudinon, J.,Abounit, S.,Ruvoen-Clouet, N.,Larson, G.,Smith, D.F.,Wimmerova, M.,Le Pendu, J.,Romer, W.,Varrot, A.,Imberty, A.
Fucose-Binding Lectin from Opportunistic Pathogen Burkholderia Ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes.
J.Biol.Chem., 287:4335-, 2012

PubMed Abstract: 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 (Sulák, O., Cioci, G., Lameignère, E., Balloy, V., Round, A., Gutsche, I., Malinovská, L., Chignard, M., Kosma, P., Aubert, D. F., Marolda, C. L., Valvano, M. A., Wimmerová, 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 αFuc1-2Gal epitopes. Crystal structures revealed that it associates as a trimer with two fucose-binding sites per monomer. The overall fold is a six-bladed β-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 μM). 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.

PubMed: 22170069
DOI: 10.1074/JBC.M111.314831

実験手法

X-RAY DIFFRACTION (1.68 Å)