Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C

Peter H. Rehse, Noriyasu Ohshima, Yuichi Nodake, Tahir H Tahirov

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The X-ray crystallographic structure of osmotically inducible Protein C from the thermophilic bacterium, Thermus thermophilus HB8, was solved to 1.6Å using the multiple wavelength anomalous dispersion method and a selenomethionine incorporated protein (Se-MAD). The crystal space group was P1 with cell dimensions of a=37.58Å, b=40.95Å, c=48.14Å, α=76.9°, β=74.0°and γ=64.1°. The two tightly interacting monomers in the asymmetric unit are related by a non-crystallographic 2-fold. The dimer structure is defined primarily by two very long anti-parallel, over-lapping α-helices at the core, with a further six-stranded anti-parallel β-sheet on the outside of the structure. With respect to the β-sheets, both A and B monomers contribute three strands each resulting in an intertwining of the structure. The active site consists of two cysteine residues from one monomer and an arginine and glutamic acid from the other. Enzymatic assays have revealed that T.thermophilus OsmC has a hydroperoxide peroxidase activity.

Original languageEnglish (US)
Pages (from-to)959-968
Number of pages10
JournalJournal of Molecular Biology
Volume338
Issue number5
DOIs
StatePublished - May 14 2004

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Selenomethionine
Thermus thermophilus
Enzyme Assays
Protein C
Hydrogen Peroxide
Peroxidase
Cysteine
Arginine
Glutamic Acid
Catalytic Domain
X-Rays
Bacteria
Proteins
mycophenolic adenine dinucleotide

Keywords

  • CHP, cumene hydroperoxide
  • DTT, 1,4-dithiothreitol
  • Ohr
  • Ohr, organic hydroperoxide resistance protein
  • OsmC
  • OsmC, osmotically inducible protein C
  • Osmotic stress
  • Peroxidase
  • X-ray crystal structure
  • tBOOH, tert-butyl hydroperoxide

ASJC Scopus subject areas

  • Virology

Cite this

Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C. / Rehse, Peter H.; Ohshima, Noriyasu; Nodake, Yuichi; Tahirov, Tahir H.

In: Journal of Molecular Biology, Vol. 338, No. 5, 14.05.2004, p. 959-968.

Research output: Contribution to journalArticle

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abstract = "The X-ray crystallographic structure of osmotically inducible Protein C from the thermophilic bacterium, Thermus thermophilus HB8, was solved to 1.6{\AA} using the multiple wavelength anomalous dispersion method and a selenomethionine incorporated protein (Se-MAD). The crystal space group was P1 with cell dimensions of a=37.58{\AA}, b=40.95{\AA}, c=48.14{\AA}, α=76.9°, β=74.0°and γ=64.1°. The two tightly interacting monomers in the asymmetric unit are related by a non-crystallographic 2-fold. The dimer structure is defined primarily by two very long anti-parallel, over-lapping α-helices at the core, with a further six-stranded anti-parallel β-sheet on the outside of the structure. With respect to the β-sheets, both A and B monomers contribute three strands each resulting in an intertwining of the structure. The active site consists of two cysteine residues from one monomer and an arginine and glutamic acid from the other. Enzymatic assays have revealed that T.thermophilus OsmC has a hydroperoxide peroxidase activity.",
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