Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Backbone 1H, 15N, and 13C Resonance Assignments and Secondary Structure of a Novel Protein OGL-20PT-358 from Hyperthermophile Thermococcus thioreducens sp. nov.

  • Wilson, Randall C. (Laboratory for Structural Biology, University of Alabama in Huntsville) ;
  • Hughes, Ronny C. (Laboratory for Structural Biology, University of Alabama in Huntsville) ;
  • Curto, Ernest V. (Laboratory for Structural Biology, University of Alabama in Huntsville) ;
  • Ng, Joseph D. (Laboratory for Structural Biology, University of Alabama in Huntsville) ;
  • Twigg, Pamela D. (Laboratory for Structural Biology, University of Alabama in Huntsville)
  • Received : 2007.05.17
  • Accepted : 2007.06.25
  • Published : 2007.12.31
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Abstract

$OGL-20P^T$-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain $OGL-20P^T$, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone $^1H$, $^{15}N$, and $^{13}C$ resonance assignments of $OGL-20P^T$-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily ${\alpha}$-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.

Keywords

References

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