Backbone assignments of1H,15N and13C resonances and secondary structure prediction of MRA1997 from Mycobacterium tuberculosis H37Rv

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 Cα and Cβ chemical shift values, the secondary structure of MRA1997 was calculated. The result revealed that secondary structure of MRA 1997 consists of one α-helix and five β-sheets. Our structural study will be a footstone towards the characterization of the three-dimensional structure of MRA1997.