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Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass
- Source :
- Scientific Reports
- Publication Year :
- 2016
- Publisher :
- Springer Science and Business Media LLC, 2016.
-
Abstract
- 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 Ca2+ ion supplementation enhances the catalytic activities of ASKA and TASKA. The crystal structures reveal the presence of four Ca2+ 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.
- Subjects :
- Models, Molecular
0301 basic medicine
Subfamily
Protein Conformation
Anoxybacillus
Maltose binding
Biology
Crystallography, X-Ray
Article
03 medical and health sciences
chemistry.chemical_compound
Ion binding
Bacterial Proteins
Hydrolase
Glycosyl
Binding site
Maltose
Binding Sites
Multidisciplinary
030102 biochemistry & molecular biology
030104 developmental biology
Biochemistry
chemistry
biology.protein
Calcium
alpha-Amylases
Apoproteins
Crystallization
Alpha-amylase
Subjects
Details
- ISSN :
- 20452322
- Volume :
- 6
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....c05e4abf368fcd6354b80099c57fc82c