1qj4

From Proteopedia

Revision as of 14:55, 5 November 2007

HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION

Overview

The X-ray crystal structure of native hydroxynitrile lyase from Hevea, brasiliensis (Hb-HNL) has been determined at 1.1 A resolution. It refined, to a final R of 11.5% for all data and an Rfree of 14.4%. The favorable, data-to-parameter ratio at atomic resolution made the refinement of, individual anisotropic displacement parameters possible. The data also, allowed a clear distinction of the alternate orientations of all histidine, and the majority of asparagine and glutamine side chains. A number of, hydrogen atoms, including one on the imidazole of the mechanistically, important His-235, became visible as peaks in a difference electron, density map. The structure revealed a discretely disordered sidechain of, Ser-80, which is part of the putative catalytic triad. Analysis of the, anisotropy indicated an increased mobility of residues near the entrance, to the active site and within the active site.

About this Structure

1QJ4 is a Single protein structure of sequence from Hevea brasiliensis with SO4 and GOL as ligands. Active as Gluconate dehydratase, with EC number 4.2.1.39 Structure known Active Site: CAT. Full crystallographic information is available from OCA.

Reference

Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis., Gruber K, Gugganig M, Wagner UG, Kratky C, Biol Chem. 1999 Jul-Aug;380(7-8):993-1000. PMID:10494852

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