Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability.,Alikhajeh J, Khajeh K, Ranjbar B, Naderi-Manesh H, Lin YH, Liu E, Guan HH, Hsieh YC, Chuankhayan P, Huang YC, Jeyaraman J, Liu MY, Chen CJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt, 2):121-9. Epub 2010 Jan 26. PMID:20124706[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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