2IHO

Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc

Summary for 2IHO

• Entry DOI: 10.2210/pdb2iho/pdb
• Descriptor: Lectin, beta-D-galactopyranose-(1-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: beta-trefoil, sugar binding protein
• Biological source: Marasmius oreades
• Total number of polymer chains: 1
• Total formula weight: 33419.69

Authors

Grahn, E.,Askarieh, G.,Holmner, A.,Tateno, H.,Winter, H.C.,Goldstein, I.J.,Krengel, U. (deposition date: 2006-09-27, release date: 2007-05-22, Last modification date: 2024-02-21)

Primary citation

Grahn, E.,Askarieh, G.,Holmner, A.,Tateno, H.,Winter, H.C.,Goldstein, I.J.,Krengel, U.
Crystal structure of the marasmius oreades mushroom lectin in complex with a xenotransplantation epitope.
J.Mol.Biol., 369:710-721, 2007

PubMed Abstract: MOA, a lectin from the mushroom Marasmius oreades, is one of the few reagents that specifically agglutinate blood group B erythrocytes. Further, it is the only lectin known to have exclusive specificity for Galalpha(1,3)Gal-containing sugar epitopes, which are antigens that pose a severe barrier to animal-to-human organ transplantation. We describe here the structure of MOA at 2.4 A resolution, in complex with the linear trisaccharide Galalpha(1,3)Galbeta(1,4)GlcNAc. The structure is dimeric, with two distinct domains per protomer: the N-terminal lectin module adopts a ricinB/beta-trefoil fold and contains three putative carbohydrate-binding sites, while the C-terminal domain serves as a dimerization interface. This latter domain, which has an unknown function, reveals a novel fold with intriguing conservation of an active site cleft. A number of indications suggest that MOA may have an enzymatic function in addition to the sugar-binding properties.

PubMed: 17442345
DOI: 10.1016/j.jmb.2007.03.016

Experimental method

X-RAY DIFFRACTION (2.41 Å)