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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.141
- 4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase.
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Reaction:
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Hydrolysis of alpha-(1->4)-D-glucosidic linkage in 4-alpha-D- {(1->4)-alpha-D-glucanosyl}(n) trehalose to yield trehalose and alpha- (1->4)-D-glucan.
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biological process
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metabolic process
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3 terms
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Biochemical function
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catalytic activity
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6 terms
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DOI no:
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J Mol Biol
301:451-464
(2000)
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PubMed id:
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Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus.
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M.D.Feese,
Y.Kato,
T.Tamada,
M.Kato,
T.Komeda,
Y.Miura,
M.Hirose,
K.Hondo,
K.Kobayashi,
R.Kuroki.
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ABSTRACT
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The crystal structure of glycosyltrehalose trehalohydrolase from the
hyperthermophilic archaeum Sulfolobus solfataricus KM1 has been solved by
multiple isomorphous replacement. The enzyme is an alpha-amylase (family 13)
with unique exo-amylolytic activity for glycosyltrehalosides. It cleaves the
alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose
and maltooligo saccharide. Unlike most other family 13 glycosidases, the enzyme
does not require Ca(2+) for activity, and it contains an N-terminal extension of
approximately 100 amino acid residues that is homologous to N-terminal domains
found in many glycosidases that recognize branched oligosaccharides.
Crystallography revealed the enzyme to exist as a homodimer covalently linked by
an intermolecular disulfide bond at residue C298. The existence of the
intermolecular disulfide bond was confirmed by biochemical analysis and
mutagenesis. The N-terminal extension forms an independent domain connected to
the catalytic domain by an extended linker. The functionally essential Ca(2+)
binding site found in the B domain of alpha-amylases and many other family 13
glycosidases was found to be replaced by hydrophobic packing interactions. The
enzyme also contains a very unusual excursion in the (beta/alpha)(8) barrel
structure of the catalytic domain. This excursion originates from the bottom of
the (beta/alpha)(8) barrel between helix 6 and strand 7, but folds upward in a
distorted alpha-hairpin structure to form a part of the substrate binding cleft
wall that is possibly critical for the enzyme's unique substrate selectivity.
Participation of an alpha-beta loop in the formation of the substrate binding
cleft is a novel feature that is not observed in other known (beta/alpha)(8)
enzymes.
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Selected figure(s)
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Figure 3.
Figure 3. Dimerization of KM1 GTHase. Stereo view of the
GTHase dimer viewed down the molecular 2-fold axis to emphasize
the intermolecular disulfide bond and the participation of the
a6b-b7 (green) and the B domain (blue) in the dimer interface.
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Figure 6.
Figure 6. Comparison of the B domains of KM1 GTHase and A.
oryzae a-amylase (TAA). The bound calcium ion of A. oryzae
a-amylase is shown as a green sphere with three surrounding
solvent ligands shown as red spheres. Residues indicated for A.
oryzae are the ligands to the calcium ion and the generally
conserved disulfide bond. Residues indicated for S. solfataricus
form the small hydrophobic core and replace the calcium binding
site in A. oryzae.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2000,
301,
451-464)
copyright 2000.
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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.Guelorget,
M.Roovers,
V.Guérineau,
C.Barbey,
X.Li,
and
B.Golinelli-Pimpaneau
(2010).
Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase.
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Nucleic Acids Res, 38,
6206-6218.
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PDB codes:
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W.Y.Chou,
W.I.Chou,
T.W.Pai,
S.C.Lin,
T.Y.Jiang,
C.Y.Tang,
and
M.D.Chang
(2010).
Feature-incorporated alignment based ligand-binding residue prediction for carbohydrate-binding modules.
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Bioinformatics, 26,
1022-1028.
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M.Palomo,
S.Kralj,
M.J.van der Maarel,
and
L.Dijkhuizen
(2009).
The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains.
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Appl Environ Microbiol, 75,
1355-1362.
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H.Yamada,
T.Tamada,
M.Kosaka,
K.Miyata,
S.Fujiki,
M.Tano,
M.Moriya,
M.Yamanishi,
E.Honjo,
H.Tada,
T.Ino,
H.Yamaguchi,
J.Futami,
M.Seno,
T.Nomoto,
T.Hirata,
M.Yoshimura,
and
R.Kuroki
(2007).
'Crystal lattice engineering,' an approach to engineer protein crystal contacts by creating intermolecular symmetry: crystallization and structure determination of a mutant human RNase 1 with a hydrophobic interface of leucines.
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Protein Sci, 16,
1389-1397.
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PDB codes:
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J.Eichler,
and
M.W.Adams
(2005).
Posttranslational protein modification in Archaea.
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Microbiol Mol Biol Rev, 69,
393-425.
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M.Beeby,
B.D.O'Connor,
C.Ryttersgaard,
D.R.Boutz,
L.J.Perry,
and
T.O.Yeates
(2005).
The genomics of disulfide bonding and protein stabilization in thermophiles.
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PLoS Biol, 3,
e309.
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PDB code:
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A.Linden,
O.Mayans,
W.Meyer-Klaucke,
G.Antranikian,
and
M.Wilmanns
(2003).
Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc.
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J Biol Chem, 278,
9875-9884.
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PDB codes:
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G.Polekhina,
A.Gupta,
B.J.Michell,
B.van Denderen,
S.Murthy,
S.C.Feil,
I.G.Jennings,
D.J.Campbell,
L.A.Witters,
M.W.Parker,
B.E.Kemp,
and
D.Stapleton
(2003).
AMPK beta subunit targets metabolic stress sensing to glycogen.
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Curr Biol, 13,
867-871.
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H.B.Fritzsche,
T.Schwede,
and
G.E.Schulz
(2003).
Covalent and three-dimensional structure of the cyclodextrinase from Flavobacterium sp. no. 92.
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Eur J Biochem, 270,
2332-2341.
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PDB code:
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S.Janecek,
B.Svensson,
and
E.A.MacGregor
(2003).
Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
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Eur J Biochem, 270,
635-645.
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E.A.MacGregor,
S.Janecek,
and
B.Svensson
(2001).
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
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Biochim Biophys Acta, 1546,
1.
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T.Yokota,
T.Tonozuka,
S.Kamitori,
and
Y.Sakano
(2001).
The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 alpha-amylases: effects of domain N on activity, specificity, stability and dimerization.
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Biosci Biotechnol Biochem, 65,
401-408.
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T.Yokota,
T.Tonozuka,
Y.Shimura,
K.Ichikawa,
S.Kamitori,
and
Y.Sakano
(2001).
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
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Biosci Biotechnol Biochem, 65,
619-626.
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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
