1GEG

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

Summary for 1GEG

• Entry DOI: 10.2210/pdb1geg/pdb
• Descriptor: ACETOIN REDUCTASE, alpha-D-glucopyranose, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: sdr family, oxidoreductase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 8
• Total formula weight: 220417.32

Authors

Otagiri, M.,Kurisu, G.,Ui, S.,Kusunoki, M. (deposition date: 2000-11-10, release date: 2001-02-28, Last modification date: 2023-12-27)

Primary citation

Otagiri, M.,Kurisu, G.,Ui, S.,Takusagawa, Y.,Ohkuma, M.,Kudo, T.,Kusunoki, M.
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.
J.Biochem., 129:205-208, 2001

PubMed Abstract: 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.

PubMed: 11173520
DOI: 10.1093/oxfordjournals.jbchem.a002845

Experimental method

X-RAY DIFFRACTION (1.7 Å)