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PDBsum entry 2j1v
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Carbohydrate-binding protein
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PDB id
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2j1v
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Contents |
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* Residue conservation analysis
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DOI no:
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J Biol Chem
281:35263-35271
(2006)
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PubMed id:
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Blood group antigen recognition by a Streptococcus pneumoniae virulence factor.
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A.B.Boraston,
D.Wang,
R.D.Burke.
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ABSTRACT
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The Streptococcus pneumoniae fucose utilization operon includes a gene encoding
a virulence factor that belongs to family 98 in the glycoside hydrolase
classification. This protein contains a C-terminal triplet of fucose binding
modules that have significant amino acid sequence identity with the Anguilla
anguilla fucolectin. Functional studies of these fucose binding modules reveal
binding to fucosylated oligosaccharides and suggest the importance of
multivalent binding. The high resolution crystal structures of ligand bound
forms of one fucose binding module uncovers the molecular basis of fucose, ABH
blood group antigen, and Lewisy antigen binding. These studies are extended by
fluorescence microscopy to show specific binding to mouse lung tissue. These
modules define a new family of carbohydrate binding modules now classified as
family 47.
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Selected figure(s)
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Figure 5.
FIGURE 5. Binding site architectures and electron density
of fucose (A), the type II H-trisaccharide (B), the blood group
A-tetrasaccharide analogue (C), and the Lewis^y antigen (D)
bound to SpX-1. Electron density maps are
maximum-likelihood(17)/ [A] (27) weighted
2F[obs] - F[calc] electron density maps contoured at 1 (0.39,
0.48, 0.23, and 0.28 electrons/Å^3) for the fucose, type
II blood group H-trisaccharide, blood group A-tetrasaccharide
analogue, and Lewis^y antigen complexes, respectively. Relevant
residues involved in binding are shown in gray stick
representation and labeled.
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Figure 6.
FIGURE 6. Hydrogen bonding schematics of fucose (A), the
type II H-trisaccharide (B), the blood group A-tetrasaccharide
analogue (C), and the Lewis^y antigen (D) bound to SpX-1.
Potential hydrogen bonds are shown as dotted lines. Waters are
shown as gray spheres. Potential hydrogen bond distances were
between 2.5 and 3.3 Å.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
35263-35271)
copyright 2006.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Guillén,
S.Sánchez,
and
R.Rodríguez-Sanoja
(2010).
Carbohydrate-binding domains: multiplicity of biological roles.
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Appl Microbiol Biotechnol,
85,
1241-1249.
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C.Montanier,
A.L.van Bueren,
C.Dumon,
J.E.Flint,
M.A.Correia,
J.A.Prates,
S.J.Firbank,
R.J.Lewis,
G.G.Grondin,
M.G.Ghinet,
T.M.Gloster,
C.Herve,
J.P.Knox,
B.G.Talbot,
J.P.Turkenburg,
J.Kerovuo,
R.Brzezinski,
C.M.Fontes,
G.J.Davies,
A.B.Boraston,
and
H.J.Gilbert
(2009).
Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.
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Proc Natl Acad Sci U S A,
106,
3065-3070.
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PDB codes:
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E.Ficko-Blean,
and
A.B.Boraston
(2009).
N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH.
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J Mol Biol,
390,
208-220.
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PDB codes:
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K.J.Gregg,
and
A.B.Boraston
(2009).
Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
133-135.
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M.A.Higgins,
G.E.Whitworth,
N.El Warry,
M.Randriantsoa,
E.Samain,
R.D.Burke,
D.J.Vocadlo,
and
A.B.Boraston
(2009).
Differential recognition and hydrolysis of host carbohydrate antigens by Streptococcus pneumoniae family 98 glycoside hydrolases.
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J Biol Chem,
284,
26161-26173.
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PDB codes:
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G.W.Moy,
S.A.Springer,
S.L.Adams,
W.J.Swanson,
and
V.D.Vacquier
(2008).
Extraordinary intraspecific diversity in oyster sperm bindin.
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Proc Natl Acad Sci U S A,
105,
1993-1998.
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K.J.Gregg,
R.Finn,
D.W.Abbott,
and
A.B.Boraston
(2008).
Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.
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J Biol Chem,
283,
12604-12613.
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PDB codes:
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K.S.Aragão,
M.Satre,
A.Imberty,
and
A.Varrot
(2008).
Structure determination of Discoidin II from Dictyostelium discoideum and carbohydrate binding properties of the lectin domain.
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Proteins,
73,
43-52.
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PDB codes:
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S.A.Shelburne,
M.T.Davenport,
D.B.Keith,
and
J.M.Musser
(2008).
The role of complex carbohydrate catabolism in the pathogenesis of invasive streptococci.
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Trends Microbiol,
16,
318-325.
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S.Farrand,
E.Hotze,
P.Friese,
S.K.Hollingshead,
D.F.Smith,
R.D.Cummings,
G.L.Dale,
and
R.K.Tweten
(2008).
Characterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domain.
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Biochemistry,
47,
7097-7107.
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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
codes are
shown on the right.
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