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Crystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAcCrystal structure of MOA, a lectin from the mushroom Marasmius oreades in complex with the trisaccharide Gal(1,3)Gal(1,4)GlcNAc
Structural highlights
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 PubMedMOA, 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. Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope.,Grahn E, Askarieh G, Holmner A, Tateno H, Winter HC, Goldstein IJ, Krengel U J Mol Biol. 2007 Jun 8;369(3):710-21. Epub 2007 Mar 15. PMID:17442345[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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