3BH4

High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase

Summary for 3BH4

• Entry DOI: 10.2210/pdb3bh4/pdb
• Related: 1BLI 1E43
• Descriptor: Alpha-amylase, CALCIUM ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: crystal structure alpha-amylase, calcium, carbohydrate metabolism, glycosidase, hydrolase, metal-binding, secreted
• Biological source: Bacillus amyloliquefaciens
• Cellular location: Secreted : P00692
• Total number of polymer chains: 2
• Total formula weight: 110171.00

Authors

Alikhajeh, J.,Khajeh, K.,Ranjbar, B.,Naderi-Manesh, H.,Lin, Y.H.,Liu, M.Y.,Chen, C.J. (deposition date: 2007-11-28, release date: 2008-12-09, Last modification date: 2023-11-01)

Primary citation

Alikhajeh, J.,Khajeh, K.,Ranjbar, B.,Naderi-Manesh, H.,Lin, Y.H.,Liu, E.,Guan, H.H.,Hsieh, Y.C.,Chuankhayan, P.,Huang, Y.C.,Jeyaraman, J.,Liu, M.Y.,Chen, C.J.
Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution: implications for thermal stability.
Acta Crystallogr.,Sect.F, 66:121-129, 2010

PubMed 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.

PubMed: 20124706
DOI: 10.1107/S1744309109051938

Experimental method

X-RAY DIFFRACTION (1.4 Å)