2FMD

Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin

Summary for 2FMD

• Entry DOI: 10.2210/pdb2fmd/pdb
• Related PRD ID: PRD_900111
• Descriptor: Lectin, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: legume lectin, beta sandwich, protein-carbohydrate complex, lectin, sugar binding protein
• Biological source: Bowringia mildbraedii
• Total number of polymer chains: 1
• Total formula weight: 26020.28

Authors

Buts, L.,Garcia-Pino, A.,Wyns, L.,Loris, R. (deposition date: 2006-01-09, release date: 2006-08-22, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)