2fmd
From Proteopedia
Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin
Overview
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.
About this Structure
2FMD is a Single protein structure of sequence from Bowringia mildbraedii. Full crystallographic information is available from OCA.
Reference
Structural basis of carbohydrate recognition by a Man(alpha1-2)Man-specific lectin from Bowringia milbraedii., Buts L, Garcia-Pino A, Wyns L, Loris R, Glycobiology. 2006 Jul;16(7):635-40. Epub 2006 Mar 27. PMID:16567368 Page seeded by OCA on Sun May 4 04:04:00 2008
