Structure of archaeal glyoxylate reductase from Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate

Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):357-65. doi: 10.1107/S0907444906055442. Epub 2007 Feb 21.


Glyoxylate reductase catalyzes the NAD(P)H-linked reduction of glyoxylate to glycolate. Here, the 1.7 A crystal structure of glyoxylate reductase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3 complexed with nicotinamide adenine dinucleotide phosphate [NADP(H)] determined by the single-wavelength anomalous dispersion (SAD) method is reported. The monomeric structure comprises the two domains typical of NAD(P)-dependent dehydrogenases: the substrate-binding domain (SBD) and the nucleotide-binding domain (NBD). The crystal structure and analytical ultracentrifugation results revealed dimer formation. In the NADP(H)-binding site, the pyrophosphate moiety and the 2'-phosphoadenosine moiety are recognized by the glycine-rich loop (residues 157-162) and by loop residues 180-182, respectively. Furthermore, the present study revealed that P. horikoshii glyoxylate reductase contains aromatic clusters and has a larger number of ion pairs and a lower percentage of hydrophobic accessible surface area than its mesophilic homologues, suggesting its thermostability mechanism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / chemistry*
  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Binding Sites
  • Dimerization
  • Molecular Sequence Data
  • NADP / chemistry*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Pyrococcus horikoshii / enzymology*
  • Sequence Alignment


  • Archaeal Proteins
  • NADP
  • Alcohol Oxidoreductases
  • glyoxylate reductase
  • glyoxylate reductase (NADP+)