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J Biol Chem, Vol. 273, Issue 31, 19859-19865, July 31, 1998

Crystal Structure of Recombinant Soybean beta -Amylase Complexed with beta -Cyclodextrin

Motoyasu Adachi, Bunzo Mikami, Tomoyuki Katsube§, and Shigeru Utsumi

From the Research Institute for Food Science, Kyoto University, Uji Kyoto 611-0011, Japan and the § Department of Domestic Science, Shimane Prefectural Shimane Women's College, Shimane 690-0044, Japan

In order to study the interaction of soybean beta -amylase with substrate, we solved the crystal structure of beta -cyclodextrin-enzyme complex and compared it with that of alpha -cyclodextrin-enzyme complex. The enzyme was expressed in Escherichia coli at a high level as a soluble and catalytically active protein. The purified recombinant enzyme had properties nearly identical to those of native soybean beta -amylase and formed the same crystals as the native enzyme. The crystal structure of recombinant enzyme complexed with beta -cyclodextrin was refined at 2.07-Å resolution with a final crystallographic R value of 15.8% (Rfree = 21.1%). The root mean square deviation in the position of C-alpha atoms between this recombinant enzyme and the native enzyme was 0.22 Å. These results indicate that the expression system established here is suitable for studying structure-function relationships of beta -amylase. The conformation of the bound beta -cyclodextrin takes an ellipsoid shape in contrast to the circular shape of the bound alpha -cyclodextrin. The cyclodextrins shared mainly two glucose binding sites, 3 and 4. The glucose residue 4 was slightly shifted from the maltose binding site. This suggests that the binding site of the cyclodextrins is important for its holding of a cleaved substrate, which enables the multiple attack mechanism of beta -amylase.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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