1v03
CRYSTAL STRUCTURE OF THE SORGHUM BICOLOR DHURRINASE 1
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OverviewOverview
Plant beta-glucosidases play a crucial role in defense against pests. They, cleave, with variable specificity, beta-glucosides to release toxic, aglycone moieties. The Sorghum bicolor beta-glucosidase isoenzyme Dhr1 has, a strict specificity for its natural substrate dhurrin, (p-hydroxy-(S)-mandelonitrile-beta-D-glucoside), whereas its close, homolog, the maize beta-glucosidase isoenzyme Glu1, which shares 72%, sequence identity, hydrolyzes a broad spectrum of substrates in addition, to its natural substrate, 2-O-beta-D-glucopyranosyl-4-hydroxy-7-methoxy-1,4-benzoxaxin-3-one., Structural data from enzyme.substrate complexes of Dhr1 show that the mode, of aglycone binding differs from that previously observed in the, homologous maize enzyme. Specifically, the data suggest that Asn(259), ... [(full description)]
About this StructureAbout this Structure
1V03 is a [Single protein] structure of sequence from [Sorghum bicolor] with BGC, IPH and CCN as [ligands]. Active as [[1]], with EC number [3.2.1.21]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate., Verdoucq L, Moriniere J, Bevan DR, Esen A, Vasella A, Henrissat B, Czjze M, J Biol Chem. 2004 Jul 23;279(30):31796-803. Epub 2004 May 17. PMID:15148317
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