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KMID : 0545119990090050619
Journal of Microbiology and Biotechnology
1999 Volume.9 No. 5 p.619 ~ p.623
Structure of the Starch-Binding Domain of Bacillus cereus ¥â-Amylase
YOON, HYE-JIN
HIRATA, AKIRA/ADACHI, MOTOYASU/SEKINE, ATSUSHI/UTSUMI, SHIGERU/MIKAMI, BUNZO
Abstract
The C-terminal starch-binding domain of Bacillus cereus ¥â-amylase expressed in Escherichia coli was purified and crystallized using the vapor diffusion method. The crystals obtained belong to a space group of P3^_221 with cell dimensions, a=b=60.20 ¡Ê, c=64.92 ¡Ê, and ¥ã=120¡Æ. The structure was determined by the molecular replacement method and refined at 1.95 ¡Ê 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 ¥â- 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 ¥â-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.
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