Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei

G Bell, RJM Russell, M Kohlhoff, R Hensel, MJ Danson, DW Hough, Garry Lindsay Taylor

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14 Citations (Scopus)

Abstract

Recombinant triosephosphate isomerase (TIM) from a hyperthermophilic Archaeon, Pyrococcus woesei, has been crystallized. Three crystal forms have been obtained: monoclinic, orthorhombic and hexagonal. The monoclinic crystals belong to space group P2(1) with cell dimensions a = 79.1, b = 89.2, c = 145.4 Angstrom and beta = 92.8 degrees, and diffract to at least 2.6 Angstrom. The orthorhombic crystals belong to space group P2(1)2(1)2 with a = 89.4, b = 155.9, c = 79.5 Angstrom, and diffract to 2.9 Angstrom. Diffraction from the hexagonal form showed extensive disorder. The monoclinic form contains two tetramers in the asymmetric unit, which are in the same orientation but related by a pseudo-centring. The orthorhombic form contains one tetramer in the asymmetric unit which is in approximately the same orientation as in the monoclinic form. Knowledge of the structure of this hyperthermostable TIM, which is tetrameric in contrast to dimeric forms previously observed, will add to the understanding of protein thermostability.

Original languageEnglish
Pages (from-to)1419-1421
Number of pages3
JournalActa Crystallographica. Section D, Biological crystallography
Volume54
Publication statusPublished - 1 Nov 1998

Keywords

  • CRYSTAL-STRUCTURE
  • ANGSTROM RESOLUTION
  • THERMOTOGA-MARITIMA
  • THERMOSTABILITY
  • STABILITY
  • ENZYME
  • DETERMINANTS
  • PROTEINS
  • FURIOSUS

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