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Structural characterization of a lectin from the mushroom Marasmius oreades in complex with the blood group B trisaccharide and calcium.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Grahn EM,Winter HC,Tateno H,Goldstein IJ,Krengel U

doi

10.1016/j.jmb.2009.04.074

subject

Has Abstract

pub_date

2009-07-17 00:00:00

pages

457-66

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(09)00541-5

journal_volume

390

pub_type

杂志文章

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