2fmd | pdb_00002fmd
Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin
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| 2fmd, resolution 1.9Å | |||||||||||||
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| Ligands: | CA and MN | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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 Thu Mar 20 16:54:13 2008
