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* Residue conservation analysis
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Enzyme class:
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E.C.2.4.1.207
- Xyloglucan:xyloglucosyl transferase.
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Reaction:
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Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.
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Gene Ontology (GO) functional annotation
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Cellular component
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apoplast
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2 terms
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Biological process
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carbohydrate metabolic process
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2 terms
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Biochemical function
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transferase activity
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4 terms
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DOI no:
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Plant Cell
16:874-886
(2004)
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PubMed id:
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Crystal structures of a poplar xyloglucan endotransglycosylase reveal details of transglycosylation acceptor binding.
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P.Johansson,
H.Brumer,
M.J.Baumann,
A.M.Kallas,
H.Henriksson,
S.E.Denman,
T.T.Teeri,
T.A.Jones.
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ABSTRACT
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Xyloglucan endotransglycosylases (XETs) cleave and religate xyloglucan polymers
in plant cell walls via a transglycosylation mechanism. Thus, XET is a key
enzyme in all plant processes that require cell wall remodeling. To provide a
basis for detailed structure-function studies, the crystal structure of Populus
tremula x tremuloides XET16A (PttXET16A), heterologously expressed in Pichia
pastoris, has been determined at 1.8-A resolution. Even though the overall
structure of PttXET16A is a curved beta-sandwich similar to other enzymes in the
glycoside hydrolase family GH16, parts of its substrate binding cleft are more
reminiscent of the distantly related family GH7. In addition, XET has a
C-terminal extension that packs against the conserved core, providing an
additional beta-strand and a short alpha-helix. The structure of XET in complex
with a xyloglucan nonasaccharide, XLLG, reveals a very favorable acceptor
binding site, which is a necessary but not sufficient prerequisite for
transglycosylation. Biochemical data imply that the enzyme requires sugar
residues in both acceptor and donor sites to properly orient the glycosidic bond
relative to the catalytic residues.
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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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T.Addington,
B.Calisto,
M.Alfonso-Prieto,
C.Rovira,
I.Fita,
and
A.Planas
(2011).
Re-engineering specificity in 1,3-1, 4-β-glucanase to accept branched xyloglucan substrates.
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Proteins, 79,
365-375.
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PDB code:
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D.D.Wong,
V.J.Chan,
A.A.McCormack,
and
S.B.Batt
(2010).
A novel xyloglucan-specific endo-beta-1,4-glucanase: biochemical properties and inhibition studies.
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Appl Microbiol Biotechnol, 86,
1463-1471.
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R.Yokoyama,
Y.Uwagaki,
H.Sasaki,
T.Harada,
Y.Hiwatashi,
M.Hasebe,
and
K.Nishitani
(2010).
Biological implications of the occurrence of 32 members of the XTH (xyloglucan endotransglucosylase/hydrolase) family of proteins in the bryophyte Physcomitrella patens.
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Plant J, 64,
645-656.
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A.Maris,
D.Suslov,
S.C.Fry,
J.P.Verbelen,
and
K.Vissenberg
(2009).
Enzymic characterization of two recombinant xyloglucan endotransglucosylase/hydrolase (XTH) proteins of Arabidopsis and their effect on root growth and cell wall extension.
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J Exp Bot, 60,
3959-3972.
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B.Mertz,
X.Gu,
and
P.J.Reilly
(2009).
Analysis of functional divergence within two structurally related glycoside hydrolase families.
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Biopolymers, 91,
478-495.
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J.R.Chen,
X.Xiong,
T.X.Wang,
J.J.Lü,
S.Y.Chen,
and
H.F.Wang
(2009).
Rapid construction of a plant RNA interference expression vector for hairpin RNA-mediated targeting using a PCR-based method.
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DNA Cell Biol, 28,
605-613.
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J.Vasur,
R.Kawai,
E.Andersson,
K.Igarashi,
M.Sandgren,
M.Samejima,
and
J.Ståhlberg
(2009).
X-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysis.
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FEBS J, 276,
3858-3869.
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M.Hrmova,
V.Farkas,
A.J.Harvey,
J.Lahnstein,
B.Wischmann,
N.Kaewthai,
I.Ezcurra,
T.T.Teeri,
and
G.B.Fincher
(2009).
Substrate specificity and catalytic mechanism of a xyloglucan xyloglucosyl transferase HvXET6 from barley (Hordeum vulgare L.).
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FEBS J, 276,
437-456.
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R.Hurtado-Guerrero,
A.W.Schüttelkopf,
I.Mouyna,
A.F.Ibrahim,
S.Shepherd,
T.Fontaine,
J.P.Latgé,
and
D.M.van Aalten
(2009).
Molecular mechanisms of yeast cell wall glucan remodeling.
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J Biol Chem, 284,
8461-8469.
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PDB codes:
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R.Schröder,
R.G.Atkinson,
and
R.J.Redgwell
(2009).
Re-interpreting the role of endo-beta-mannanases as mannan endotransglycosylase/hydrolases in the plant cell wall.
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Ann Bot (Lond), 104,
197-204.
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X.Lu,
Y.Chu,
Q.Wu,
Y.Gu,
F.Han,
and
W.Yu
(2009).
Cloning, expression and characterization of a new agarase-encoding gene from marine Pseudoalteromonas sp.
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Biotechnol Lett, 31,
1565-1570.
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C.Zhou,
A.N.Lakso,
T.L.Robinson,
and
S.Gan
(2008).
Isolation and characterization of genes associated with shade-induced apple abscission.
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Mol Genet Genomics, 280,
83-92.
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T.Takeda,
J.G.Miller,
and
S.C.Fry
(2008).
Anionic derivatives of xyloglucan function as acceptor but not donor substrates for xyloglucan endotransglucosylase activity.
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Planta, 227,
893-905.
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K.Piens,
A.M.Henriksson,
F.Gullfot,
M.Lopez,
R.Fauré,
F.M.Ibatullin,
T.T.Teeri,
H.Driguez,
and
H.Brumer
(2007).
Glycosynthase activity of hybrid aspen xyloglucan endo-transglycosylase PttXET16-34 nucleophile mutants.
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Org Biomol Chem, 5,
3971-3978.
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N.Nishikubo,
T.Awano,
A.Banasiak,
V.Bourquin,
F.Ibatullin,
R.Funada,
H.Brumer,
T.T.Teeri,
T.Hayashi,
B.Sundberg,
and
E.J.Mellerowicz
(2007).
Xyloglucan endo-transglycosylase (XET) functions in gelatinous layers of tension wood fibers in poplar--a glimpse into the mechanism of the balancing act of trees.
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Plant Cell Physiol, 48,
843-855.
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V.S.Van Sandt,
H.Stieperaere,
Y.Guisez,
J.P.Verbelen,
and
K.Vissenberg
(2007).
XET activity is found near sites of growth and cell elongation in bryophytes and some green algae: new insights into the evolution of primary cell wall elongation.
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Ann Bot, 99,
39-51.
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G.Michel,
P.Nyval-Collen,
T.Barbeyron,
M.Czjzek,
and
W.Helbert
(2006).
Bioconversion of red seaweed galactans: a focus on bacterial agarases and carrageenases.
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Appl Microbiol Biotechnol, 71,
23-33.
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J.Vasur,
R.Kawai,
A.M.Larsson,
K.Igarashi,
M.Sandgren,
M.Samejima,
and
J.Ståhlberg
(2006).
X-ray crystallographic native sulfur SAD structure determination of laminarinase Lam16A from Phanerochaete chrysosporium.
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Acta Crystallogr D Biol Crystallogr, 62,
1422-1429.
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PDB code:
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K.N.Neustroev,
A.M.Golubev,
M.L.Sinnott,
R.Borriss,
M.Krah,
H.Brumer,
E.V.Eneyskaya,
S.Shishlyannikov,
K.A.Shabalin,
V.T.Peshechonov,
V.G.Korolev,
and
A.A.Kulminskaya
(2006).
Transferase and hydrolytic activities of the laminarinase from Rhodothermus marinus and its M133A, M133C, and M133W mutants.
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Glycoconj J, 23,
501-511.
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M.Saladié,
J.K.Rose,
D.J.Cosgrove,
and
C.Catalá
(2006).
Characterization of a new xyloglucan endotransglucosylase/hydrolase (XTH) from ripening tomato fruit and implications for the diverse modes of enzymic action.
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Plant J, 47,
282-295.
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N.Farrokhi,
R.A.Burton,
L.Brownfield,
M.Hrmova,
S.M.Wilson,
A.Bacic,
and
G.B.Fincher
(2006).
Plant cell wall biosynthesis: genetic, biochemical and functional genomics approaches to the identification of key genes.
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Plant Biotechnol J, 4,
145-167.
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R.Kawai,
K.Igarashi,
M.Yoshida,
M.Kitaoka,
and
M.Samejima
(2006).
Hydrolysis of beta-1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium.
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Appl Microbiol Biotechnol, 71,
898-906.
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M.Strohmeier,
M.Hrmova,
M.Fischer,
A.J.Harvey,
G.B.Fincher,
and
J.Pleiss
(2004).
Molecular modeling of family GH16 glycoside hydrolases: potential roles for xyloglucan transglucosylases/hydrolases in cell wall modification in the poaceae.
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Protein Sci, 13,
3200-3213.
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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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