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Backbone assignments of 1H, 15N and 13C resonances and secondary structure prediction of MRA1997 from Mycobacterium tuberculosis H37Rv

  • Kim, Hyojung (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Kim, Yena (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Ki-Young (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University) ;
  • Lee, Bong-Jin (Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University)
  • Received : 2015.04.15
  • Accepted : 2015.06.01
  • Published : 2015.06.30

Abstract

MRA1997 is a 76-residue conserved hypothetical protein of Mycobacterium tuberculosis H37Ra, one of the most pathogenic bacterial species and the causative agent of tuberculosis. In this study, the sequence-specific backbone resonance assignment of MRA1997 was performed using NMR spectroscopy. Approximately 88.3% of the total resonances could be unambiguously assigned. By analyzing deviations of the $C{\alpha}$ and $C{\beta}$ chemical shift values, the secondary structure of MRA1997 was calculated. The result revealed that secondary structure of MRA 1997 consists of one ${\alpha}$-helix and five ${\beta}$-sheets. Our structural study will be a footstone towards the characterization of the three-dimensional structure of MRA1997.

Keywords

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Cited by

  1. Secondary structure analysis of MRA1997 from Mycobacterium tuberculosis and characterization of DNA binding property vol.20, pp.2, 2016, https://doi.org/10.6564/JKMRS.2016.20.2.036