The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum

R J M RUSSELL, D W HOUGH, M J DANSON, G L TAYLOR

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183 Citations (Scopus)

Abstract

Background: The Archaea constitute a phylogenetically distinct, evolutionary domain and comprise organisms that live under environmental extremes of temperature, salinity and/or anaerobicity. Different members of the thermophilic Archaea tolerate temperatures in the range 55-110 degrees C, and the comparison of the structures of their enzymes with the structurally homogolous enzymes of mesophilic organisms (optimum growth temperature range 15-45 degrees C) may provide important information on the structural basis of protein thermostability. We have chosen citrate synthase, the first enzyme of the citric acid cycle, as a model enzyme for such studies.

Results: We have determined the crystal structure of Thermoplasma acidophilum citrate synthase to 2.5 Angstrom and have compared it with the citrate synthase from pig heart, with which it shares a high degree of structural homology, but little sequence identity (20%).

Conclusions: The three-dimensional structural comparison of thermophilic and mesophilic citrate synthases has permitted catalytic and substrate-binding residues to be tentatively assigned in the archaeal, thermophilic enzyme, and has identified structural features that may be responsible for its thermostability.

Original languageEnglish
Pages (from-to)1157-1167
Number of pages11
JournalStructure
Volume2
Issue number12
Publication statusPublished - 15 Dec 1994

Keywords

  • ARCHAEA
  • CITRATE SYNTHASE
  • CRYSTAL STRUCTURE
  • THERMOPHILE
  • THERMOPLASMA ACIDOPHILUM
  • ALPHA-HELIX STABILITY
  • PROTEIN-STRUCTURE
  • ESCHERICHIA-COLI
  • CRYSTALLOGRAPHIC REFINEMENT
  • SECONDARY STRUCTURE
  • SEQUENCE
  • MUTATIONS
  • MODELS
  • GENE
  • DEHYDROGENASE

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