2BT9

Lectin from Ralstonia solanacearum complexed with Me-fucoside

2BT9 の概要

• エントリーDOI: 10.2210/pdb2bt9/pdb
• 関連するPDBエントリー: 2BS5 2BS6
• 分子名称: LECTIN, methyl alpha-L-fucopyranoside (3 entities in total)
• 機能のキーワード: lectin, sugar recognition, beta-propeller
• 由来する生物種: RALSTONIA SOLANACEARUM
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30317.78

構造登録者

Mitchell, E.P.,Kostlanova, N.,Wimmerova, M.,Imberty, A. (登録日: 2005-05-27, 公開日: 2005-06-02, 最終更新日: 2024-05-08)

主引用文献

Kostlanova, N.,Mitchell, E.P.,Lortat-Jacob, H.,Oscarson, S.,Lahmann, M.,Gilboa-Garber, N.,Chambat, G.,Wimmerova, M.,Imberty, A.
The fucose-binding lectin from Ralstonia solanacearum. A new type of beta-propeller architecture formed by oligomerization and interacting with fucoside, fucosyllactose, and plant xyloglucan.
J. Biol. Chem., 280:27839-27849, 2005

PubMed Abstract: Plant pathogens, like animal ones, use protein-carbohydrate interactions in their strategy for host recognition, attachment, and invasion. The bacterium Ralstonia solanacearum, which is distributed worldwide and causes lethal wilt in many agricultural crops, was shown to produce a potent L-fucose-binding lectin, R. solanacearum lectin, a small protein of 90 amino acids with a tandem repeat in its amino acid sequence. In the present study, surface plasmon resonance experiments conducted on a series of oligosaccharides show a preference for binding to alphaFuc1-2Gal and alphaFuc1-6Gal epitopes. Titration microcalorimetry demonstrates the presence of two binding sites per monomer and an unusually high affinity of the lectin for alphaFuc1-2Gal-containing oligosaccharides (KD = 2.5 x 10(-7) M for 2-fucosyllactose). R. solanacearum lectin has been crystallized with a methyl derivative of fucose and with the highest affinity ligand, 2-fucosyllactose. X-ray crystal structures, the one with alpha-methyl-fucoside being at ultrahigh resolution, reveal that each monomer consists of two small four-stranded anti-parallel beta-sheets. Trimerization through a 3-fold or pseudo-3-fold axis generates a six-bladed beta-propeller architecture, very similar to that previously described for the fungal lectin of Aleuria aurantia. This is the first report of a beta-propeller formed by oligomerization and not by sequential domains. Each monomer presents two fucose binding sites, resulting in six symmetrically arranged sugar binding sites for the beta-propeller. Crystals were also obtained for a mutated lectin complexed with a fragment of xyloglucan, a fucosylated polysaccharide from the primary cell wall of plants, which may be the biological target of the lectin.

PubMed: 15923179
DOI: 10.1074/jbc.M505184200

実験手法

X-RAY DIFFRACTION (0.94 Å)