Molecules and Cells

  • 제24권3호
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  • Pages.437-440
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  • 2007
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  • 1016-8478(pISSN)
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  • 0219-1032(eISSN)
한국분자세포생물학회 (Korean Society for Molecular and Cellular Biology)
권호 표지

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)
  • 투고 : 2007.05.17
  • 심사 : 2007.06.25
  • 발행 : 2007.12.31
⟨ 이전 논문 다음 논문 ⟩

초록

$OGL-20P^T$-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.

키워드

참고문헌

  1. Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 https://doi.org/10.1093/nar/25.17.3389
  2. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
  3. Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352
  4. Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665 https://doi.org/10.1021/ja00052a088
  5. Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., et al. (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. J. Mol. Biol. 280, 933-952 https://doi.org/10.1006/jmbi.1998.1852
  6. Muhandiram, D. R. and Kay, L. E. (1994) Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. 103B, 203-216
  7. Pikuta, E. V., Marsic, D., Itoh, T., Bej, A. K., Tang, J., et al. (2007) Thermococcus thioreducens sp. nov., a novel hyperthermophilic, obligately sulfur-reducing archaeon from a deep-sea hydrothermal vent. Int. J. Syst. Evol. Microbiol. 57, 1612-1618 https://doi.org/10.1099/ijs.0.65057-0
  8. Wishart, D. S. and Sykes, B. D. (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4, 171-180