| Literature DB >> 20124706 |
Jahan Alikhajeh1, Khosro Khajeh, Bijan Ranjbar, Hossein Naderi-Manesh, Yi Hung Lin, Enhung Liu, Hong Hsiang Guan, Yin Cheng Hsieh, Phimonphan Chuankhayan, Yen Chieh Huang, Jeyakanthan Jeyaraman, Ming Yih Liu, Chun Jung Chen.
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.Entities:
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Year: 2010 PMID： 20124706 PMCID： PMC2815676 DOI： 10.1107/S1744309109051938
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091