The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum

J JOHN, S J CRENNELL, D W HOUGH, M J DANSON, G L TAYLOR

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60 Citations (Scopus)

Abstract

Background: The archaea are a group of organisms distinct from bacteria and eukaryotes. Structures of proteins from archaea are of interest because they function in extreme environments and because structural studies may reveal evolutionary relationships between proteins. The enzyme glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum is of additional interest because it is involved in an unusual pathway of sugar metabolism.

Results: We have determined the crystal structure of this glucose dehydrogenase to 2.9 angstrom resolution. The monomer comprises a central nucleotide-binding domain, common to other nucleotide-binding dehydrogenases, flanked by the catalytic domain. Unexpectedly, we observed significant structural homology between the catalytic domain of horse fiver alcohol dehydrogenase and T. acidopbilum glucose dehydrogenase.

Conclusions: The structural homology between glucose dehydrogenase and alcohol dehydrogenase suggests an evolutionary relationship between these enzymes. The quaternary structure of glucose dehydrogenase may provide a model for other tetrameric alcohol/polyol dehydrogenases. The predicted mode of nucleotide binding provides a plausible explanation for the observed dual-cofactor specificity, the molecular basis of which can be tested by site-directed mutagenesis.

Original languageEnglish
Pages (from-to)385-393
Number of pages9
JournalStructure
Volume2
Issue number5
Publication statusPublished - 15 May 1994

Keywords

  • ARCHAEON
  • CRYSTAL STRUCTURE
  • DUAL-COFACTOR SPECIFIC
  • GLUCOSE DEHYDROGENASE
  • THERMOPLASMA-ACIDOPHILUM
  • ALCOHOL-DEHYDROGENASE
  • PROTEIN MODELS
  • SEQUENCE
  • RESOLUTION
  • FEATURES
  • LOCATION
  • DOMAINS
  • GENE

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