3A28

Crystal structure of L-2,3-butanediol dehydrogenase

Summary for 3A28

• Entry DOI: 10.2210/pdb3a28/pdb
• Related: 1geg
• Descriptor: L-2.3-butanediol dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, BETA-MERCAPTOETHANOL, ... (5 entities in total)
• Functional Keywords: chiral substrate recognition, oxidoreductase
• Biological source: Brevibacterium saccharolyticum
• Total number of polymer chains: 8
• Total formula weight: 223058.76

Authors

Otagiri, M.,Kurisu, G.,Ui, S.,Kusunoki, M. (deposition date: 2009-05-02, release date: 2009-12-15, Last modification date: 2023-11-01)

Primary citation

Otagiri, M.,Ui, S.,Takusagawa, Y.,Ohtsuki, T.,Kurisu, G.,Kusunoki, M.
Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases
Febs Lett., 584:219-223, 2010

PubMed Abstract: 2,3-butanediol dehydrogenase (BDH) catalyzes the NAD-dependent redox reaction between acetoin and 2,3-butanediol. There are three types of homologous BDH, each stereospecific for both substrate and product. To establish how these homologous enzymes possess differential stereospecificities, we determined the crystal structure of l-BDH with a bound inhibitor at 2.0 A. Comparison with the inhibitor binding mode of meso-BDH highlights the role of a hydrogen-bond from a conserved Trp residue(192). Site-directed mutagenesis of three active site residues of meso-BDH, including Trp(190), which corresponds to Trp(192) of L-BDH, converted its stereospecificity to that of L-BDH. This result confirms the importance of conserved residues in modifying the stereospecificity of homologous enzymes.

PubMed: 19941855
DOI: 10.1016/j.febslet.2009.11.068

Experimental method

X-RAY DIFFRACTION (2 Å)