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PDBsum entry 5a2c
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PDB id:
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Hydrolase
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Title:
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Crystal structure of anoxybacillus alpha-amylase provides insights into a new glycosyl hydrolase subclass
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Structure:
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Alpha-amylase. Chain: a. Fragment: truncated protein, residues 24-478. Engineered: yes. Other_details: catalytic domain a with tim barrel fold (residues 26 to 139,187 to 393), domain b (residues 140 to 186), and domain c with an all-alpha-beta fold (residues 394 to 475)
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Source:
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Anoxybacillus sp.. Organism_taxid: 654421. Strain: sk3-4. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: isolated from sungai klah hot spring malaysia
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Resolution:
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1.90Å
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R-factor:
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0.159
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R-free:
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0.209
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Authors:
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C.L.Ng,K.P.Chai,N.F.Othman,A.H.Teh,K.L.Ho,K.G.Chan,K.M.Goh
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Key ref:
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K.P.Chai
et al.
(2016).
Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass.
Sci Rep,
6,
23126.
PubMed id:
DOI:
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Date:
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17-May-15
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Release date:
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30-Mar-16
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PROCHECK
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Headers
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References
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I1VWH9
(I1VWH9_9BACI) -
Alpha-amylase from Anoxybacillus ayderensis
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Seq:
Struc:
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505 a.a.
450 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.3.2.1.1
- alpha-amylase.
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Reaction:
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Endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.
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DOI no:
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Sci Rep
6:23126
(2016)
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PubMed id:
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Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass.
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K.P.Chai,
N.F.Othman,
A.H.Teh,
K.L.Ho,
K.G.Chan,
M.S.Shamsir,
K.M.Goh,
C.L.Ng.
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ABSTRACT
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A new subfamily of glycosyl hydrolase family GH13 was recently proposed for
α-amylases from Anoxybacillus species (ASKA and ADTA), Geobacillus
thermoleovorans (GTA, Pizzo, and GtamyII), Bacillus aquimaris (BaqA), and 95
other putative protein homologues. To understand this new GH13 subfamily, we
report crystal structures of truncated ASKA (TASKA). ASKA is a thermostable
enzyme capable of producing high levels of maltose. Unlike GTA, biochemical
analysis showed that Ca(2+) ion supplementation enhances the catalytic
activities of ASKA and TASKA. The crystal structures reveal the presence of four
Ca(2+) ion binding sites, with three of these binding sites are highly conserved
among Anoxybacillus α-amylases. This work provides structural insights into
this new GH13 subfamily both in the apo form and in complex with maltose.
Furthermore, structural comparison of TASKA and GTA provides an overview of the
conformational changes accompanying maltose binding at each subsite.
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