1e56
From Proteopedia
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CRYSTAL STRUCTURE OF THE INACTIVE MUTANT MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE ZMGLUE191D IN COMPLEX WITH THE NATURAL SUBSTRATE DIMBOA-BETA-D-GLUCOSIDE
Overview
The mechanism and the site of substrate (i.e., aglycone) recognition and, specificity were investigated in maize beta-glucosidase (Glu1) by x-ray, crystallography by using crystals of a catalytically inactive mutant, (Glu1E191D) in complex with the natural substrate, 2-O-beta-d-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one, (DIMBOAGlc), the free aglycone DIMBOA, and competitive inhibitor, para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin). The structures of, these complexes and of the free enzyme were solved at 2.1-, 2.1-, 2.0-, and 2.2-A resolution, respectively. The structural data from the complexes, allowed us to visualize an intact substrate, free aglycone, or a, competitive inhibitor in the slot-like active site of a beta-glucosidase., These data show that the aglycone ... [(full description)]
About this Structure
1E56 is a [Single protein] structure of sequence from [[1]] with GLC and HBO as [ligands]. Active as [Beta-glucosidase], with EC number [3.2.1.21]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes., Czjzek M, Cicek M, Zamboni V, Bevan DR, Henrissat B, Esen A, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13555-60. PMID:11106394 [[Category: ]]
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