3a28

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Crystal structure of L-2,3-butanediol dehydrogenase

Structural highlights

3a28 is a 8 chain structure with sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:BME, MG, NAD
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BUDC_CORGT Catalyzes the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol (L-BD) in the presence of NADH. To a lesser extent, can also catalyze the irreversible reduction of diacetyl to (S)-acetoin. Cannot oxidize meso-BD, D-BD, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, and n-propanol. Cannot reduce (R)-acetoin, acetol, dihydroxyacetone and 2,4-pentanedione.[REFERENCE:1][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases.,Otagiri M, Ui S, Takusagawa Y, Ohtsuki T, Kurisu G, Kusunoki M FEBS Lett. 2010 Jan 4;584(1):219-23. Epub . PMID:19941855[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
3 reviews cite this structure
Production of C2-C4 diols from renewable bioresources: new metabolic pathways and metabolic engineering strategies.
Zhang et al. (2017)
2 more
10 other articles
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References

  1. ↑ Takusagawa Y, Otagiri M, Ui S, Ohtsuki T, Mimura A, Ohkuma M, Kudo T. Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli. Biosci Biotechnol Biochem. 2001 Aug;65(8):1876-8. PMID:11577733
  2. ↑ 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. 2010 Jan 4;584(1):219-23. Epub . PMID:19941855 doi:10.1016/j.febslet.2009.11.068

Contents


PDB ID 3a28

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