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PDBsum entry 3vsr
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PDB id:
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Hydrolase
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Title:
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Microbacterium saccharophilum k-1 beta-fructofuranosidase catalytic domain
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Structure:
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Beta-fructofuranosidase. Chain: a. Fragment: unp residues 37-532. Engineered: yes
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Source:
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Arthrobacter. Organism_taxid: 160970. Strain: k-1. Gene: bff. Expressed in: bacillus subtilis. Expression_system_taxid: 1423.
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Resolution:
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2.00Å
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R-factor:
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0.196
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R-free:
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0.241
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Authors:
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T.Tonozuka,A.Tamaki,G.Yokoi,T.Miyazaki,M.Ichikawa,A.Nishikawa,Y.Ohta, Y.Hidaka,K.Katayama,Y.Hatada,T.Ito,K.Fujita
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Key ref:
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T.Tonozuka
et al.
(2012).
Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase.
Enzyme Microb Technol,
51,
359-365.
PubMed id:
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Date:
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08-May-12
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Release date:
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22-Aug-12
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PROCHECK
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Headers
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References
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Q8VW87
(Q8VW87_9MICO) -
Beta-fructofuranosidase from Microbacterium saccharophilum
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Seq:
Struc:
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578 a.a.
493 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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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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Enzyme Microb Technol
51:359-365
(2012)
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PubMed id:
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Crystal structure of a lactosucrose-producing enzyme, Arthrobacter sp. K-1 β-fructofuranosidase.
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T.Tonozuka,
A.Tamaki,
G.Yokoi,
T.Miyazaki,
M.Ichikawa,
A.Nishikawa,
Y.Ohta,
Y.Hidaka,
K.Katayama,
Y.Hatada,
T.Ito,
K.Fujita.
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ABSTRACT
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Arthrobacter sp. K-1 β-fructofuranosidase (ArFFase), a glycoside hydrolase
family 68 enzyme, catalyzes the hydrolysis and transfructosylation of sucrose.
ArFFase is useful for producing a sweetener, lactosucrose
(4(G)-β-d-galactosylsucrose). The primary structure of ArFFase is homologous to
those of levansucrases, although ArFFase catalyzes mostly hydrolysis when
incubated with sucrose alone, even at high concentration. Here, we determined
the crystal structure of ArFFase in unliganded form and complexed with fructose.
ArFFase consisted of a five-bladed β-propeller fold as observed in
levansucrases. The structure of ArFFase was most similar to that of
Gluconacetobacter diazotrophicus levansucrase (GdLev). The structure of the
catalytic cleft of ArFFase was also highly homologous to that of GdLev. However,
two amino acid residues, Tyr232 and Pro442 in ArFFase, were not conserved
between them. A tunnel observed at the bottom of the catalytic cleft of ArFFase
may serve as a water drain or its reservoir.
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