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PDBsum entry 1jf5
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of thermoactinomyces vulgaris r-47 alpha-amylase 2 mutant f286a
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Structure:
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Alpha amylase ii. Chain: a, b. Synonym: neopullulanase. Engineered: yes. Mutation: yes
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Source:
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Thermoactinomyces vulgaris. Organism_taxid: 2026. Strain: r-47. Expressed in: escherichia coli. Expression_system_taxid: 562
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Biol. unit:
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Dimer (from
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Resolution:
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3.20Å
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R-factor:
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0.214
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R-free:
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0.273
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Authors:
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A.Ohtaki,S.Kondo,Y.Shimura,T.Tonozuka,Y.Sakano,S.Kamitori
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Key ref:
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A.Ohtaki
et al.
(2001).
Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs.
Carbohydr Res,
334,
309-313.
PubMed id:
DOI:
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Date:
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20-Jun-01
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Release date:
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22-May-02
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PROCHECK
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Headers
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References
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Q08751
(NEPU2_THEVU) -
Neopullulanase 2 from Thermoactinomyces vulgaris
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Seq:
Struc:
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585 a.a.
585 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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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.3.2.1.135
- neopullulanase.
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Reaction:
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Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose).
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DOI no:
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Carbohydr Res
334:309-313
(2001)
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PubMed id:
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Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs.
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A.Ohtaki,
S.Kondo,
Y.Shimura,
T.Tonozuka,
Y.Sakano,
S.Kamitori.
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ABSTRACT
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Phe286 located in the center of the active site of alpha-amylase 2 from
Thermoactinomyces vulgaris R-47 (TVAII) plays an important role in the substrate
recognition for cyclomaltooligosaccharides (cyclodextrins). The X-ray structures
of mutant TVAIIs with the replacement of Phe286 by Ala (F286A) and Tyr (F286Y)
were determined at 3.2 A resolution. Their structures have no significant
differences from that of the wild-type enzyme. The kinetic analyses of
Phe286-replaced variants showed that the variants with non-aromatic residues,
Ala (F286A) and Leu (F286L), have lower enzymatic activities than those with
aromatic residues, Tyr (F286Y) and Trp (F286W), and the replacement of Phe286
affects enzymatic activities for CDs more than those for starch.
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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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K.Tang,
R.S.Kobayashi,
V.Champreda,
L.Eurwilaichitr,
and
S.Tanapongpipat
(2008).
Isolation and characterization of a novel thermostable neopullulanase-like enzyme from a hot spring in Thailand.
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Biosci Biotechnol Biochem,
72,
1448-1456.
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T.Tonozuka,
A.Sogawa,
M.Yamada,
N.Matsumoto,
H.Yoshida,
S.Kamitori,
K.Ichikawa,
M.Mizuno,
A.Nishikawa,
and
Y.Sakano
(2007).
Structural basis for cyclodextrin recognition by Thermoactinomyces vulgaris cyclo/maltodextrin-binding protein.
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FEBS J,
274,
2109-2120.
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PDB codes:
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A.Ohtaki,
M.Mizuno,
T.Tonozuka,
Y.Sakano,
and
S.Kamitori
(2004).
Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.
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J Biol Chem,
279,
31033-31040.
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PDB codes:
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M.Mizuno,
T.Tonozuka,
A.Uechi,
A.Ohtaki,
K.Ichikawa,
S.Kamitori,
A.Nishikawa,
and
Y.Sakano
(2004).
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
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Eur J Biochem,
271,
2530-2538.
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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
