3EF2

Structure of the Marasmius oreades mushroom lectin (MOA) in complex with Galalpha(1,3)[Fucalpha(1,2)]Gal and Calcium.

Summary for 3EF2

• Entry DOI: 10.2210/pdb3ef2/pdb
• Descriptor: Agglutinin, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]alpha-D-galactopyranose, ... (6 entities in total)
• Functional Keywords: lectin, beta-trefoil, calcium-binding, carbohydrate-binding, sugar-binding, sugar binding protein
• Biological source: Marasmius oreades
• Total number of polymer chains: 4
• Total formula weight: 136245.51

Authors

Grahn, E.M.,Goldstein, I.J.,Krengel, U. (deposition date: 2008-09-08, release date: 2009-06-30, Last modification date: 2023-11-15)

Primary citation

Grahn, E.M.,Winter, H.C.,Tateno, H.,Goldstein, I.J.,Krengel, U.
Structural Characterization of a Lectin from the Mushroom Marasmius oreades in Complex with the Blood Group B Trisaccharide and Calcium.
J.Mol.Biol., 390:457-466, 2009

PubMed Abstract: MOA (Marasmius oreades agglutinin), a lectin isolated from fruiting bodies of the mushroom M. oreades, specifically binds nonreducing terminal Galalpha(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galalpha(1,3)Galbeta(1,4)GlcNAc and the branched blood group B determinant Galalpha(1,3)[Fucalpha(1,2)]Gal. Here, we present the crystal structure of MOA in complex with the blood group B trisaccharide solved at 1.8 A resolution. To our knowledge, this is the first blood-group-B-specific structure reported in complex with a blood group B determinant. The carbohydrate ligand binds to all three binding sites of the N-terminal beta-trefoil domain. Also, in this work, Ca(2+) was included in the crystals, and binding of Ca(2+) to the MOA homodimer altered the conformation of the C-terminal domain by opening up the cleft containing a putative catalytic site.

PubMed: 19426740
DOI: 10.1016/j.jmb.2009.04.074

Experimental method

X-RAY DIFFRACTION (1.8 Å)