PDBsum entry: 3ef2

Sugar binding protein

PDB-id: 3ef2

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Description

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PROCHECK

Protein chains

292 a.a. *

Ligands

FUC-GAL-GLA ×8

FUC-GLA-GLA ×4

ACT ×4

Metal ions

_CA ×16

Waters ×1258

* Residue conservation analysis

Tools

Clefts Calculation

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PDB id:

3ef2

Name:

Sugar binding protein

Title:

Structure of the marasmius oreades mushroom lectin (moa) in complex with galalpha(1,3)[fucalpha(1,2)]gal and calcium.

Structure:

Agglutinin. Chain: a, b, c, d. Synonym: lectin. Engineered: yes

Source:

Marasmius oreades. Organism_taxid: 181124. Expressed in: escherichia coli. Expression_system_taxid: 562

UniProt:

Chain : ()

Resolution:

1.80Å

R-factor:

0.166

R-free:

0.189

Authors:

E.M.Grahn,I.J.Goldstein,U.Krengel

Key ref:

E.M.Grahn et al. (2009). 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. [PubMed id: 19426740] [DOI: 10.1016/j.jmb.2009.04.074]

Date:

08-Sep-08

Release date:

30-Jun-09

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Surface

Key reference

DOI no: 10.1016/j.jmb.2009.04.074

J Mol Biol 390:457-466 (2009)

PubMed id: 19426740

Structural Characterization of a Lectin from the Mushroom Marasmius oreades in Complex with the Blood Group B Trisaccharide and Calcium.

E.M.Grahn, H.C.Winter, H.Tateno, I.J.Goldstein, U.Krengel.

ABSTRACT

MOA, a lectin isolated from the fruiting bodies of the mushroom Marasmius oreades, specifically binds non-reducing terminal Galalpha(1,3)Gal-carbohydrates, such as 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 alters the conformation of the C-terminal domain by opening up the cleft containing a putative catalytic site.