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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.26
- Beta-fructofuranosidase.
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Reaction:
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Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides.
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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3 terms
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Biological process
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metabolic process
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5 terms
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Biochemical function
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hydrolase activity
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5 terms
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DOI no:
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Acta Crystallogr D Biol Crystallogr
62:1555-1563
(2006)
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PubMed id:
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X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana.
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M.Verhaest,
W.Lammens,
K.Le Roy,
B.De Coninck,
C.J.De Ranter,
A.Van Laere,
W.Van den Ende,
A.Rabijns.
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ABSTRACT
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Cell-wall invertases play crucial roles during plant development. They hydrolyse
sucrose into its fructose and glucose subunits by cleavage of the alpha1-beta2
glycosidic bond. Here, the structure of the Arabidopsis thaliana cell-wall
invertase 1 (AtcwINV1; gene accession code At3g13790) is described at a
resolution of 2.15 A. The structure comprises an N-terminal fivefold
beta-propeller domain followed by a C-terminal domain formed by two beta-sheets.
The active site is positioned in the fivefold beta-propeller domain, containing
the nucleophile Asp23 and the acid/base catalyst Glu203 of the
double-displacement enzymatic reaction. The function of the C-terminal domain
remains unknown. Unlike in other GH 32 family enzyme structures known to date,
in AtcwINV1 the cleft formed between both domains is blocked by Asn299-linked
carbohydrates. A preliminary site-directed mutagenesis experiment (Asn299Asp)
removed the glycosyl chain but did not alter the activity profile of the enzyme.
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Selected figure(s)
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Figure 3.
Figure 3 The different bonds between the Asn299 N-linked
carbohydrates in invertase (a). The carbohydrate configuration
was obtained through electron-density map interpretation. The
stereo figure (b) shows the glycosylation chain (orange) on
Asn299 (red). This figure was prepared with PyMOL (DeLano,
2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System.
DeLano Scientific, San Carlos, USA. http://www.pymol.org .]).
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Figure 5.
Figure 5 Active site of invertase. The key residues of the
active site and one glycerol molecule are displayed. Bonding
interactions are shown as dashed lines, while the spheres
represent water molecules. The corresponding distances are given
in Å. This figure was prepared with PyMOL (DeLano,
2002[DeLano, W. L. (2002). The PyMOL Molecular Graphics System.
DeLano Scientific, San Carlos, USA. http://www.pymol.org .]).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
1555-1563)
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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A.Bujacz,
M.Jedrzejczak-Krzepkowska,
S.Bielecki,
I.Redzynia,
and
G.Bujacz
(2011).
Crystal structures of the apo form of β-fructofuranosidase from Bifidobacterium longum and its complex with fructose.
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FEBS J, 278,
1728-1744.
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PDB codes:
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M.A.Rodríguez,
O.F.Sánchez,
and
C.J.Alméciga-Díaz
(2011).
Gene cloning and enzyme structure modeling of the Aspergillus oryzae N74 fructosyltransferase.
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Mol Biol Rep, 38,
1151-1161.
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E.Wang,
X.Xu,
L.Zhang,
H.Zhang,
L.Lin,
Q.Wang,
Q.Li,
S.Ge,
B.R.Lu,
W.Wang,
and
Z.He
(2010).
Duplication and independent selection of cell-wall invertase genes GIF1 and OsCIN1 during rice evolution and domestication.
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BMC Evol Biol, 10,
108.
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M.Hothorn,
W.Van den Ende,
W.Lammens,
V.Rybin,
and
K.Scheffzek
(2010).
Structural insights into the pH-controlled targeting of plant cell-wall invertase by a specific inhibitor protein.
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Proc Natl Acad Sci U S A, 107,
17427-17432.
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PDB code:
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W.Van den Ende,
W.Lammens,
A.Van Laere,
L.Schroeven,
and
K.Le Roy
(2009).
Donor and acceptor substrate selectivity among plant glycoside hydrolase family 32 enzymes.
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FEBS J, 276,
5788-5798.
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G.Meng,
and
K.Fütterer
(2008).
Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucrase.
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BMC Struct Biol, 8,
16.
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PDB codes:
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J.Mátrai,
W.Lammens,
A.Jonckheer,
K.Le Roy,
A.Rabijns,
W.Van den Ende,
and
M.De Maeyer
(2008).
An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: an X-ray crystallography and docking study.
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Proteins, 71,
552-564.
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PDB code:
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T.Canam,
F.Unda,
and
S.D.Mansfield
(2008).
Heterologous expression and functional characterization of two hybrid poplar cell-wall invertases.
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Planta, 228,
1011-1019.
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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
