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Structural Characterization of a Lectin from the  Mushroom Marasmius oreades in Complex with the  Blood Group B Trisaccharide and Calcium
Örebro University, School of Science and Technology. (Biokemi)
University of Michigan.
University of Michigan.
University of Michigan.
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2009 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 390, no 3, 457-466 p.Article in journal (Refereed) Published
Abstract [en]

MOA (Marasmius oreades agglutinin), a lectin isolated from fruiting bodies of the mushroom M. oreades, specifically binds nonreducing terminal Galα(1,3)Gal carbohydrates, such as that which occurs in the xenotransplantation epitope Galα(1,3)Galβ(1,4)GlcNAc and the branched blood group B determinant Galα(1,3)[Fucα(1,2)]Gal. Here, we present the crystal structure of MOA in complex with the blood group B trisaccharide solved at 1.8 Å 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 β-trefoil domain. Also, in this work, Ca2+ was included in the crystals, and binding of Ca2+ to the MOA homodimer altered the conformation of the C-terminal domain by opening up the cleft containing a putative catalytic site.

Place, publisher, year, edition, pages
Amsterdam: Academic Press, 2009. Vol. 390, no 3, 457-466 p.
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Biochemistry and Molecular Biology Structural Biology
Research subject
Biochemistry
Identifiers
URN: urn:nbn:se:oru:diva-8666DOI: 10.1016/j.jmb.2009.04.074ISI: 000267906400010PubMedID: 19426740Scopus ID: 2-s2.0-67449099042OAI: oai:DiVA.org:oru-8666DiVA: diva2:279386
Available from: 2009-12-03 Created: 2009-12-03 Last updated: 2017-02-23Bibliographically approved

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Grahn, Elin M.
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CiteExportLink to record
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Citation style
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