2fmd | pdb_00002fmd

Structural basis of carbohydrate recognition by Bowringia milbraedii seed agglutinin

spinqualitylabelsall models 2fmd, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fmd is a 1 chain structure with sequence from Leucomphalos mildbraedii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, MN, MAN NonStd Res: ASX Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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