ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 59 citations in OpenAlex.
- Exploring a novel GH13_5 α-amylase from Jeotgalibacillus malaysiensis D5AMB Express · 2024Article
- Structural and Functional Characterization ofMolecules (Basel, Switzerland) · 2023Article
- Structural and functional adaptation in extremophilic microbial α-amylases.Biophysical reviews · 2022Review
- Molecular cloning, expression, and biochemical characterization of a novel cold-active α-amylase from Bacillus sp. dsh19-1.Extremophiles : life under extreme conditions · 2018Article
- Property Improvement of α-Amylase fromFood technology and biotechnology · 2018Article
- Functional and cooperative stabilization of a two-metal (Ca, Zn) center in α-amylase derived from Flavobacteriaceae species.Scientific reports · 2017Article
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- Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus α-amylase at 1.9 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2015Article
- α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.Cellular and molecular life sciences : CMLS · 2014Review
- Close relationship of a novel Flavobacteriaceae α-amylase with archaeal α-amylases and good potentials for industrial applications.Biotechnology for biofuels · 2014Article
- Sequence and structural investigation of a novel psychrophilic α-amylase from Glaciozyma antarctica PI12 for cold-adaptation analysis.Journal of molecular modeling · 2013Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The crystal structure of Bacillus amyloliquefaciens alpha-amylase (BAA) at 1.4 A resolution revealed ambiguities in the thermal adaptation of homologous proteins in this family. The final model of BAA is composed of two molecules in a back-to-back orientation, which is likely to be a consequence of crystal packing. Despite a high degree of identity, comparison of the structure of BAA with those of other liquefying-type alpha-amylases indicated moderate discrepancies at the secondary-structural level. Moreover, a domain-displacement survey using anisotropic B-factor and domain-motion analyses implied a significant contribution of domain B to the total flexibility of BAA, while visual inspection of the structure superimposed with that of B. licheniformis alpha-amylase (BLA) indicated higher flexibility of the latter in the central domain A. Therefore, it is suggested that domain B may play an important role in liquefying alpha-amylases, as its rigidity offers a substantial improvement in thermostability in BLA compared with BAA.
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