1dwo
From Proteopedia
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CRYSTAL STRUCTURE OF HYDROXYNITRILE LYASE FROM MANIHOT ESCULENTA IN COMPLEX WITH SUBSTRATES ACETONE AND CHLOROACETONE:IMPLICATIONS FOR THE MECHANISM OF CYANOGENESIS
Overview
The crystal structures of hydroxynitrile lyase from Manihot esculenta, (MeHNL) complexed with the native substrate acetone and substrate analogue, chloroacetone have been determined and refined at 2.2 A resolution. The, substrates are positioned in the active site by hydrogen-bond interactions, of the carbonyl O atom with Thr11 OG, Ser80 OG and, to a lesser extent, Cys81 SG. These studies support a mechanism for cyanogenesis as well as, for the stereospecific MeHNL-catalyzed formation of (S)-cyanohydrins, which closely resembles the base-catalyzed chemical reaction of HCN with, carbonyl compounds.
About this Structure
1DWO is a [Single protein] structure of sequence from [Manihot esculenta] with ACN as [ligand]. Active as [[1]], with EC number [4.2.1.37]. Full crystallographic information is available from [OCA].
Reference
Structure of hydroxynitrile lyase from Manihot esculenta in complex with substrates acetone and chloroacetone: implications for the mechanism of cyanogenesis., Lauble H, Forster S, Miehlich B, Wajant H, Effenberger F, Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):194-200. PMID:11173464
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