 |
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Sugar binding protein
|
PDB id
|
|
|
|
2iho
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Sugar binding protein
|
 |
|
Title:
|
 |
Crystal structure of moa, a lectin from the mushroom marasmi 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.
|
|
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.Goldste 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:
DOI:
|
 |
|
Date:
|
 |
|
27-Sep-06
|
Release date:
|
22-May-07
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
Q8X123
(Q8X123_9AGAR) -
Agglutinin
|
|
|
|
Seq: Struc:
|
 |
 |
 |
293 a.a.
292 a.a.
|
|
|
|
|
|
|
 |
 |
|
|
|
|
|
|
 |
|
 |
|
 |
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
 |
 |
 |
|
 |
 |
 |
 |
|
 |
|
Biochemical function
|
metal ion binding
|
1 term
|
 |
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
J Mol Biol
369:710-721
(2007)
|
|
PubMed id:
|
|
|
|
|
| |
|
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
|
 |
|
|
|
 |
J.P.Yang,
X.X.Ma,
Y.X.He,
W.F.Li,
Y.Kang,
R.Bao,
Y.Chen,
and
C.Z.Zhou
(2011).
Crystal structure of the 30K protein from the silkworm Bombyx mori reveals a new member of the β-trefoil superfamily.
|
| |
J Struct Biol, 175,
97.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
G.Sulzenbacher,
V.Roig-Zamboni,
W.J.Peumans,
P.Rougé,
E.J.Van Damme,
and
Y.Bourne
(2010).
Crystal structure of the GalNAc/Gal-specific agglutinin from the phytopathogenic ascomycete Sclerotinia sclerotiorum reveals novel adaptation of a beta-trefoil domain.
|
| |
J Mol Biol, 400,
715-723.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
I.J.Goldstein
(2010).
My Favorite Enzyme: For love of lectins.
|
| |
IUBMB Life, 62,
247-250.
|
 |
|
|
|
|
 |
M.Agostino,
M.S.Sandrin,
P.E.Thompson,
E.Yuriev,
and
P.A.Ramsland
(2010).
Identification of preferred carbohydrate binding modes in xenoreactive antibodies by combining conformational filters and binding site maps.
|
| |
Glycobiology, 20,
724-735.
|
 |
|
|
|
|
 |
E.M.Grahn,
H.C.Winter,
H.Tateno,
I.J.Goldstein,
and
U.Krengel
(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.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
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.
|
 |
|
|
|
|
 |
J.Pohleven,
N.Obermajer,
J.Sabotic,
S.Anzlovar,
K.Sepcić,
J.Kos,
B.Kralj,
B.Strukelj,
and
J.Brzin
(2009).
Purification, characterization and cloning of a ricin B-like lectin from mushroom Clitocybe nebularis with antiproliferative activity against human leukemic T cells.
|
| |
Biochim Biophys Acta, 1790,
173-181.
|
 |
|
|
|
|
 |
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.
|
 |
|
|
|
|
 |
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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
|