Structure of D-lactate dehydrogenase from Aquifex aeolicus complexed with NAD(+) and lactic acid (or pyruvate)

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Dec 1;65(Pt 12):1209-13. doi: 10.1107/S1744309109044935. Epub 2009 Nov 27.

Abstract

The crystal structure of D-lactate dehydrogenase from Aquifex aeolicus (aq_727) was determined to 2.12 A resolution in space group P2(1)2(1)2(1), with unit-cell parameters a = 90.94, b = 94.43, c = 188.85 A. The structure was solved by molecular replacement using the coenzyme-binding domain of Lactobacillus helveticus D-lactate dehydrogenase and contained two homodimers in the asymmetric unit. Each subunit of the homodimer was found to be in a ;closed' conformation with the NADH cofactor bound to the coenzyme-binding domain and with a lactate (or pyruvate) molecule bound at the interdomain active-site cleft.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteria / enzymology*
  • Bacteria / genetics
  • Catalytic Domain
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Genes, Bacterial
  • Lactate Dehydrogenases / chemistry*
  • Lactate Dehydrogenases / genetics
  • Lactic Acid / chemistry
  • Lactobacillus helveticus / enzymology
  • Models, Molecular
  • NAD / chemistry
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Subunits
  • Pyruvic Acid / chemistry
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Static Electricity

Substances

  • Protein Subunits
  • Recombinant Proteins
  • NAD
  • Lactic Acid
  • Pyruvic Acid
  • Lactate Dehydrogenases
  • D-lactate dehydrogenase

Associated data

  • PDB/3KB6
  • PDB/R3KB6SF