1ex1
From Proteopedia
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BETA-D-GLUCAN EXOHYDROLASE FROM BARLEY
Overview
BACKGROUND: Cell walls of the starchy endosperm and young vegetative, tissues of barley (Hordeum vulgare) contain high levels of, (1-->3,1-->4)-beta-D-glucans. The (1-->3,1-->4)-beta-D-glucans are, hydrolysed during wall degradation in germinated grain and during wall, loosening in elongating coleoptiles. These key processes of plant, development are mediated by several polysaccharide endohydrolases and, exohydrolases. RESULTS:. The three-dimensional structure of barley, beta-D-glucan exohydrolase isoenzyme ExoI has been determined by X-ray, crystallography. This is the first reported structure of a family 3, glycosyl hydrolase. The enzyme is a two-domain, globular protein of 605, amino acid residues and is N-glycosylated at three sites. The first 357, residues constitute an ... [(full description)]
About this Structure
1EX1 is a [Single protein] structure of sequence from [Hordeum vulgare] with NAG and GLC as [ligands]. Active as [Glucan 1,3-beta-glucosidase], with EC number [3.2.1.58]. Structure known Active Site: GBS. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of a barley beta-D-glucan exohydrolase, a family 3 glycosyl hydrolase., Varghese JN, Hrmova M, Fincher GB, Structure. 1999 Feb 15;7(2):179-90. PMID:10368285
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