1e1f
From Proteopedia
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CRYSTAL STRUCTURE OF A MONOCOT (MAIZE ZMGLU1) BETA-GLUCOSIDASE IN COMPLEX WITH P-NITROPHENYL-BETA-D-THIOGLUCOSIDE
Overview
The maize beta-glucosidase isoenzymes ZMGlu1 and ZMGlu2 hydrolyse the, abundant natural substrate DIMBOAGlc, (2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxazin-3-one), whose aglycone DIMBOA (2,4-hydroxy-7-methoxy-1,4-benzoxazin-3-one) is the, major defence chemical protecting seedlings and young plant parts against, herbivores and other pests. The two isoenzymes hydrolyse DIMBOAGlc with, similar kinetics but differ from each other and their sorghum homologues, with respect to specificity towards other substrates. To gain insights, into the mechanism of substrate (i.e. aglycone) specificity between the, two maize isoenzymes and their sorghum homologues, ZMGlu1 was produced in, Escherichia coli, purified, crystallized and its structure solved at 2.5, Angstrom resolution by X-ray ... [(full description)]
About this Structure
1E1F is a [Single protein] structure of sequence from [Zea mays] with PSG as [ligand]. Active as [[1]], with EC number [3.2.1.21]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a monocotyledon (maize ZMGlu1) beta-glucosidase and a model of its complex with p-nitrophenyl beta-D-thioglucoside., Czjzek M, Cicek M, Zamboni V, Burmeister WP, Bevan DR, Henrissat B, Esen A, Biochem J. 2001 Feb 15;354(Pt 1):37-46. PMID:11171077
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