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PDBsum entry 2x0d
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* Residue conservation analysis
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J Mol Biol
397:436-447
(2010)
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PubMed id:
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Structural basis of substrate binding in WsaF, a rhamnosyltransferase from Geobacillus stearothermophilus.
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K.Steiner,
G.Hagelueken,
P.Messner,
C.Schäffer,
J.H.Naismith.
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ABSTRACT
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Carbohydrate polymers are medically and industrially important. The S-layer of
many Gram-positive organisms comprises protein and carbohydrate polymers and
forms an almost paracrystalline array on the cell surface. Not only is this
array important for the bacteria but it has potential application in the
manufacture of commercially important polysaccharides and glycoconjugates as
well. The S-layer glycoprotein glycan from Geobacillus stearothermophilus NRS
2004/3a is mainly composed of repeating units of three rhamnose sugars linked by
alpha-1,3-, alpha-1,2-, and beta-1,2-linkages. The formation of the
beta-1,2-linkage is catalysed by the enzyme WsaF. The rational use of this
system is hampered by the fact that WsaF and other enzymes in the pathway share
very little homology to other enzymes. We report the structural and biochemical
characterisation of WsaF, the first such rhamnosyltransferase to be
characterised. Structural work was aided by the surface entropy reduction
method. The enzyme has two domains, the N-terminal domain, which binds the
acceptor (the growing rhamnan chain), and the C-terminal domain, which binds the
substrate (dTDP-beta-l-rhamnose). The structure of WsaF bound to dTDP and
dTDP-beta-l-rhamnose coupled to biochemical analysis identifies the residues
that underlie catalysis and substrate recognition. We have constructed and
tested by site-directed mutagenesis a model for acceptor recognition.
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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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R.Ristl,
K.Steiner,
K.Zarschler,
S.Zayni,
P.Messner,
and
C.Schäffer
(2011).
The s-layer glycome-adding to the sugar coat of bacteria.
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Int J Microbiol,
2011,
0.
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C.Luley-Goedl,
and
B.Nidetzky
(2010).
Carbohydrate synthesis by disaccharide phosphorylases: reactions, catalytic mechanisms and application in the glycosciences.
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Biotechnol J,
5,
1324-1338.
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K.Zarschler,
B.Janesch,
M.Pabst,
F.Altmann,
P.Messner,
and
C.Schäffer
(2010).
Protein tyrosine O-glycosylation--a rather unexplored prokaryotic glycosylation system.
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Glycobiology,
20,
787-798.
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S.M.Batt,
T.Jabeen,
A.K.Mishra,
N.Veerapen,
K.Krumbach,
L.Eggeling,
G.S.Besra,
and
K.Fütterer
(2010).
Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB'.
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J Biol Chem,
285,
37741-37752.
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PDB codes:
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T.Kowatz,
J.P.Morrison,
M.E.Tanner,
and
J.H.Naismith
(2010).
The crystal structure of the Y140F mutant of ADP-L-glycero-D-manno-heptose 6-epimerase bound to ADP-beta-D-mannose suggests a one base mechanism.
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Protein Sci,
19,
1337-1343.
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PDB codes:
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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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Links
