2FMD

Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin

2FMD の概要

• エントリーDOI: 10.2210/pdb2fmd/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900111
• 分子名称: Lectin, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: legume lectin, beta sandwich, protein-carbohydrate complex, lectin, sugar binding protein
• 由来する生物種: Bowringia mildbraedii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26020.28

構造登録者

Buts, L.,Garcia-Pino, A.,Wyns, L.,Loris, R. (登録日: 2006-01-09, 公開日: 2006-08-22, 最終更新日: 2024-11-13)

主引用文献

Buts, L.,Garcia-Pino, A.,Wyns, L.,Loris, R.
Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii.
Glycobiology, 16:635-640, 2006

PubMed Abstract: The crystal structure of the seed lectin from the tropical legume Bowringia milbraedii was determined in complex with the disaccharide ligand Man(alpha1-2)Man. In solution, the protein exhibits a dynamic dimer-tetramer equilibrium, consistent with the concanavalin A-type tetramer observed in the crystal. Contacts between the tetramers are mediated almost exclusively through the carbohydrate ligand, resulting in a crystal lattice virtually identical to that of the concanavalin-A:Man(alpha1-2)Man complex, even though both proteins have less than 50% sequence identity. The disaccharide binds exclusively in a "downstream" binding mode, with the non-reducing mannose occupying the monosaccharide-binding site. The reducing mannose is bound in a predominantly polar subsite involving Tyr131, Gln218, and Tyr219.

PubMed: 16567368
DOI: 10.1093/glycob/cwj109

実験手法

X-RAY DIFFRACTION (1.9 Å)