Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Structure of the Starch-Binding Domain of Bacillus cereus $\beta-Amylase$

  • Yoon, Hye-Jin (Research Institute for Food Science, Kyoto University) ;
  • Akira, Hirata (Research Institute for Food Science, Kyoto University) ;
  • Motoyasu, Adachi (Research Institute for Food Science, Kyoto University) ;
  • Atsushi, Sekine (Research Institute for Food Science, Kyoto University) ;
  • Shigeru, Utsumi (Research Institute for Food Science, Kyoto University) ;
  • Bunzo, Mikami (Research Institute for Food Science, Kyoto University)
  • Published : 1999.10.01
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Abstract

The C-terminal starch-binding domain of Bacillus cereus $\beta$-amylase expressed in Escherichia coli was purified and crystallized using the vapor diffusion method. The crystals obtained belong to a space group of $P3_2$ 21 with cell dimensions, a=b=60.20${\AA},\; c=64.92{\AA},\; and \; \gamma = 120^{\circ}$ The structure was determined by the molecular replacement method and refined at 1.95 ${\AA}$, with R-factors of 0.181. The final model of the starch-binding domain comprised 99 amino acid residues and 108 water molecules. The starch-binding domain had a secondary structure of two 4-stranded antiparallel p-sheets similar to domain E of cyclodextrin glucanotransferase and the C-terminal starch-binding domain of glucoamylase. A comparison of the structures of these starch-binding domains revealed that the separated starch-binding domain of Bacillus cereus $\beta-Amylase$had only one starch-binding site (site 1) in contrast to two sites (site 1 and site 2) reported in the domains of cyclodextrin glucanotransferase and glucoamylase.

Keywords

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