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PDBsum entry 2fv0
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.179
- gellan tetrasaccharide unsaturated glucuronosyl hydrolase.
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Reaction:
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beta-D-Delta4-GlcA-(1->4)-beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc + H2O = beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc + 5-dehydro-4-deoxy-D- glucuronate
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beta-D-Delta(4)-GlcA-(1->4)-beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc
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+
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H2O
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=
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beta-D-Glc-(1->4)-alpha-L-Rha-(1->3)-D-Glc
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+
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5-dehydro-4-deoxy-D- glucuronate
Bound ligand (Het Group name = )
matches with 84.62% similarity
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Biochem Biophys Res Commun
344:253-262
(2006)
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PubMed id:
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Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1.
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T.Itoh,
W.Hashimoto,
B.Mikami,
K.Murata.
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ABSTRACT
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Bacterial unsaturated glucuronyl hydrolases (UGLs) together with polysaccharide
lyases are responsible for the complete depolymerization of mammalian
extracellular matrix glycosaminoglycans. UGL acts on various oligosaccharides
containing unsaturated glucuronic acid (DeltaGlcA) at the nonreducing terminus
and releases DeltaGlcA through hydrolysis. In this study, we demonstrate the
substrate recognition mechanism of the UGL of Bacillus sp. GL1 by determining
the X-ray crystallographic structure of its substrate-enzyme complexes. The
tetrasaccharide-enzyme complex demonstrated that at least four subsites are
present in the active pocket. Although several amino acid residues are crucial
for substrate binding, the enzyme strongly recognizes DeltaGlcA at subsite -1
through the formation of hydrogen bonds and stacking interactions, and prefers
N-acetyl-d-galactosamine and glucose rather than N-acetyl-d-glucosamine as a
residue accommodated in subsite +1, due to the steric hindrance.
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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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Y.Maruyama,
Y.Nakamichi,
T.Itoh,
B.Mikami,
W.Hashimoto,
and
K.Murata
(2009).
Substrate specificity of streptococcal unsaturated glucuronyl hydrolases for sulfated glycosaminoglycan.
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J Biol Chem,
284,
18059-18069.
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PDB code:
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H.Ravalason,
G.Jan,
D.Mollé,
M.Pasco,
P.M.Coutinho,
C.Lapierre,
B.Pollet,
F.Bertaud,
M.Petit-Conil,
S.Grisel,
J.C.Sigoillot,
M.Asther,
and
I.Herpoël-Gimbert
(2008).
Secretome analysis of Phanerochaete chrysosporium strain CIRM-BRFM41 grown on softwood.
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Appl Microbiol Biotechnol,
80,
719-733.
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K.Murata,
S.Kawai,
B.Mikami,
and
W.Hashimoto
(2008).
Superchannel of bacteria: biological significance and new horizons.
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Biosci Biotechnol Biochem,
72,
265-277.
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T.Itoh,
W.Hashimoto,
B.Mikami,
and
K.Murata
(2006).
Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism.
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J Biol Chem,
281,
29807-29816.
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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
code is
shown on the right.
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Links
