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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.156
- Oligosaccharide reducing-end xylanase.
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Gene Ontology (GO) functional annotation
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Biological process
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metabolic process
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4 terms
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Biochemical function
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catalytic activity
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5 terms
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DOI no:
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J Biol Chem
280:17180-17186
(2005)
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PubMed id:
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Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125.
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S.Fushinobu,
M.Hidaka,
Y.Honda,
T.Wakagi,
H.Shoun,
M.Kitaoka.
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ABSTRACT
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Reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125
(Rex) hydrolyzes xylooligosaccharides whose degree of polymerization is greater
than or equal to 3, releasing the xylose unit at the reducing end. It is a
unique exo-type glycoside hydrolase that recognizes the xylose unit at the
reducing end in a very strict manner, even discriminating the beta-anomeric
hydroxyl configuration from the alpha-anomer or 1-deoxyxylose. We have
determined the crystal structures of Rex in unliganded and complex forms at
1.35-2.20-A resolution and revealed the structural aspects of its three subsites
ranging from -2 to +1. The structure of Rex was compared with those of endo-type
enzymes in glycoside hydrolase subfamily 8a (GH-8a). The catalytic machinery of
Rex is basically conserved with other GH-8a enzymes. However, subsite +2 is
blocked by a barrier formed by a kink in the loop before helix alpha10. His-319
in this loop forms a direct hydrogen bond with the beta-hydroxyl of xylose at
subsite +1, contributing to the specific recognition of anomers at the reducing
end.
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Selected figure(s)
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Figure 2.
FIG. 2. Ribbon diagrams of the GH-8a enzymes. The catalytic
residues, ligand molecules, and metal ions are shown as black
sticks, a ball-and-stick model, and spheres, respectively. a,
side view of the (  / )[6] barrel of Rex. b,
top view of the barrel in a. The position of the [10]
helix is indicated. c, top view of the barrel of the wild-type
pXyl complexed with a xylose at subsite +4. The side chain of
the catalytic proton donor (Glu78) is positioned differently
from in the other two enzymes. d, top view of the barrel of
CelA. A part of the cellopentaose molecule (subsites -3 to -1
out of -3 to +2) and the cellotriose molecule (subsites +1 to
+3) are shown.
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Figure 5.
FIG. 5. Schematic drawing of the active sites in the
WT-xylose (a) and E70A-xylobiose (b) structures.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2005,
280,
17180-17186)
copyright 2005.
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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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A.Pollet,
J.A.Delcour,
and
C.M.Courtin
(2010).
Structural determinants of the substrate specificities of xylanases from different glycoside hydrolase families.
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Crit Rev Biotechnol, 30,
176-191.
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A.Pollet,
J.Schoepe,
E.Dornez,
S.V.Strelkov,
J.A.Delcour,
and
C.M.Courtin
(2010).
Functional analysis of glycoside hydrolase family 8 xylanases shows narrow but distinct substrate specificities and biotechnological potential.
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Appl Microbiol Biotechnol, 87,
2125-2135.
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D.B.Jordan,
and
K.Wagschal
(2010).
Properties and applications of microbial beta-D-xylosidases featuring the catalytically efficient enzyme from Selenomonas ruminantium.
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Appl Microbiol Biotechnol, 86,
1647-1658.
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M.Hidaka,
S.Fushinobu,
Y.Honda,
T.Wakagi,
H.Shoun,
and
M.Kitaoka
(2010).
Structural explanation for the acquisition of glycosynthase activity.
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J Biochem, 147,
237-244.
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PDB codes:
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W.Suginta,
D.Chuenark,
M.Mizuhara,
and
T.Fukamizo
(2010).
Novel β-N-acetylglucosaminidases from Vibrio harveyi 650: cloning, expression, enzymatic properties, and subsite identification.
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BMC Biochem, 11,
40.
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M.Fukuda,
S.Watanabe,
J.Kaneko,
Y.Itoh,
and
Y.Kamio
(2009).
The membrane lipoprotein LppX of Paenibacillus sp. strain W-61 serves as a molecular chaperone for xylanase of glycoside hydrolase family 11 during secretion across the cytoplasmic membrane.
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J Bacteriol, 191,
1641-1649.
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S.Lagaert,
S.Van Campenhout,
A.Pollet,
T.M.Bourgois,
J.A.Delcour,
C.M.Courtin,
and
G.Volckaert
(2007).
Recombinant expression and characterization of a reducing-end xylose-releasing exo-oligoxylanase from Bifidobacterium adolescentis.
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Appl Environ Microbiol, 73,
5374-5377.
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N.N.Aronson,
and
B.A.Halloran
(2006).
Optimum substrate size and specific anomer requirements for the reducing-end glycoside hydrolase di-N-acetylchitobiase.
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Biosci Biotechnol Biochem, 70,
1537-1541.
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Y.Yasutake,
S.Kawano,
K.Tajima,
M.Yao,
Y.Satoh,
M.Munekata,
and
I.Tanaka
(2006).
Structural characterization of the Acetobacter xylinum endo-beta-1,4-glucanase CMCax required for cellulose biosynthesis.
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Proteins, 64,
1069-1077.
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PDB code:
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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
