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Sugar binding protein PDB-id
2iho
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Protein chain
292 a.a. *
Ligands
NAG-GAL-GAL ×2
Waters ×170

* Residue conservation analysis
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PDB id: 2iho
Name: Sugar binding protein
Title: Crystal structure of moa, a lectin from the mushroom marasmius oreades in complex with the trisaccharide gal(1, 3)gal(1,4)glcnac

Structure:
Lectin. Chain: a. Synonym: agglutinin. Engineered: yes

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

UniProt:
Q8X123 (Q8X123_9AGAR) Pfam  
Seq:
Struc:
Seq: 293 a.a.
Struc: 292 a.a.
Key:    Secondary structure

Resolution:
2.41Å

R-factor:
0.192

R-free:
0.211

Authors:
E.Grahn,G.Askarieh,A.Holmner,H.Tateno,H.C.Winter, I.J.Goldstein,U.Krengel

Key ref:
E.Grahn et al. (2007). Crystal structure of the marasmius oreades mushroom lectin in complex with a xenotransplantation epitope.. J Mol Biol, 369, 710-721. [PubMed id: 17442345] [DOI: 10.1016/j.jmb.2007.03.016]

Date:
27-Sep-06

Release date:
22-May-07
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    Key reference    
 
 
DOI no: 10.1016/j.jmb.2007.03.016 J Mol Biol 369:710-721 (2007)
PubMed id: 17442345  
 
 
Crystal structure of the marasmius oreades mushroom lectin in complex with a xenotransplantation epitope.
E.Grahn, G.Askarieh, A.Holmner, H.Tateno, H.C.Winter, I.J.Goldstein, U.Krengel.
 
  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.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. A stereo representation of the MOA carbohydrate-binding site in complex with the trisaccharide Galα(1,3)Galβ(1,4)GlcNAc. (a) The sugar ligand (black) bound to the α-site and the residues important for sugar binding are shown as stick models. The experimental electron density map (F[obs]) is contoured at 1.0 σ. (b) An overview of the protein–ligand interactions in the α-site. The trisaccharide (red) and the residues involved in direct and indirect hydrogen bonds (cutoff at 3.4 Å) are shown as stick models. Water molecules (W) are depicted as blue spheres. (c) A corresponding overview of the protein–ligand interactions in the β-site. This Figure as well as Figures 2(a), (b), (d), 3 and 4 were made using PyMoL [http://pymol.sourceforge.net/].
Figure 3.
Figure 3. Comparison of the binding sites. (a) Superimposed backbone trace for the three binding sites α (blue), β (green) and γ (pink). The backbone trace is embedded in a surface representation of the α-site shown in light gray. For Asp40 and the residues exhibiting the largest differences in sugar binding, the side-chains are included in the picture. Likewise, the bound trisaccharides are shown as black (α-site) and grey (β-site) stick models. (b) A close-up view of the salt-bridge between Asp40 in the α-site loop and Lys265 from the C-terminal domain.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2007, 369, 710-721) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19292877 H.Hemmi, A.Kuno, S.Ito, R.Suzuki, T.Hasegawa, and J.Hirabayashi (2009).
NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris.
  FEBS J, 276, 2095-2105.  
18533830 J.Rincones, L.M.Scarpari, M.F.Carazzolle, J.M.Mondego, E.F.Formighieri, J.G.Barau, G.G.Costa, D.M.Carraro, H.P.Brentani, L.A.Vilas-Boas, B.V.de Oliveira, M.Sabha, R.Dias, J.M.Cascardo, R.A.Azevedo, L.W.Meinhardt, and G.A.Pereira (2008).
Differential gene expression between the biotrophic-like and saprotrophic mycelia of the witches' broom pathogen Moniliophthora perniciosa.
  Mol Plant Microbe Interact, 21, 891-908.  
17674202 K.A.Wearne, H.C.Winter, and I.J.Goldstein (2008).
Temporal changes in the carbohydrates expressed on BG01 human embryonic stem cells during differentiation as embryoid bodies.
  Glycoconj J, 25, 121-136.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.