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1gxs
From Proteopedia
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Revision as of 13:17, 30 October 2007
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CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM SORGHUM BICOLOR IN COMPLEX WITH INHIBITOR BENZOIC ACID: A NOVEL CYANOGENIC ENZYME
Overview
The crystal structure of the hydroxynitrile lyase from Sorghum bicolor, (SbHNL) in complex with the inhibitor benzoic acid has been determined at, 2.3 A resolution and refined to a crystallographic R-factor of 16.5%. The, SbHNL sequence places the enzyme in the alpha/beta hydrolase family where, the active site nucleophile is predicted to be organized in a, characteristic pentapeptide motif which is part of the active site, strand-turn-helix motif. In SbHNL, however, a unique two-amino acid, deletion is next to the putative active site Ser158, removing thereby the, putative oxyanion hole-forming Tyr residue. The presented X-ray structure, shows that the overall folding pattern of SbHNL is similar to that of the, closely related wheat serine carboxypeptidase (CPD-WII); however, the, ... [(full description)]
About this Structure
1GXS is a [Single protein] structure of sequence from [Sorghum bicolor] with NAG, BEZ and DKA as [ligands]. Active as [Hydroxymandelonitrile lyase], with EC number [4.1.2.11]. Structure known Active Site: CA1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of hydroxynitrile lyase from Sorghum bicolor in complex with the inhibitor benzoic acid: a novel cyanogenic enzyme., Lauble H, Miehlich B, Forster S, Wajant H, Effenberger F, Biochemistry. 2002 Oct 8;41(40):12043-50. PMID:12356304
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