期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 66, 期 -, 页码 121-129出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109051938
关键词
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资金
- research council of Tarbiat Modares University
- National Synchrotron Radiation Research Center (NSRRC)
- National Science Council (NSC) in Taiwan [NSRRC 963RSB02, NSC 95-2311-B213-001-MY3, NSC 95-2923-B-213-001-MY3]
The crystal structure of Bacillus amyloliquefaciens alpha-amylase (BAA) at 1.4 angstrom 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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