1geg

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Revision as of 13:52, 20 November 2007

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spinqualitylabelsall models 1geg, resolution 1.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYATAL STRUCTURE ANALYSIS OF MESO-2,3-BUTANEDIOL DEHYDROGENASE

Overview

The crystal structure of a ternary complex of meso-2,3-butanediol, dehydrogenase with NAD+ and a competitive inhibitor, mercaptoethanol, has, been determined at 1.7 A resolution by means of molecular replacement and, refined to a final R-factor of 0.194. The overall structure is similar to, those of the other short chain dehydrogenase/reductase enzymes. The NAD+, binding site, and the positions of catalytic residues Ser139, Tyr152, and, Lys156 are also conserved. The crystal structure revealed that, mercaptoethanol bound specifically to meso-2,3-butanediol dehydrogenase., Two residues around the active site, Gln140 and Gly183, forming hydrogen, bonds with the inhibitor, are important but not sufficient for, distinguishing stereoisomerism of a chiral substrate.

About this Structure

1GEG is a Single protein structure of sequence from Klebsiella pneumoniae with GLC, MG, NAD and BME as ligands. Active as Acetoin dehydrogenase, with EC number 1.1.1.5 Full crystallographic information is available from OCA.

Reference

Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms., Otagiri M, Kurisu G, Ui S, Takusagawa Y, Ohkuma M, Kudo T, Kusunoki M, J Biochem (Tokyo). 2001 Feb;129(2):205-8. PMID:11173520

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