Abstract
Tuberculosis is an infectious disease caused by Mycobacterium tuberculosis, which triggers severe pulmonary diseases. Recently, multidrug/extensively drug-resistant tuberculosis strains have emerged and continue to threaten global health. Because of the development of drug-resistant tuberculosis, there is an urgent need for novel antibiotics to treat these drug-resistant bacteria. In light of the clinical importance of M. tuberculosis, 2067 structures of M. tuberculsosis proteins have been determined. Among them, 52 structures have been solved and studied using solution nuclear magnetic resonance (NMR). The functional details based on structural analysis of M. tuberculosis using NMR can provide essential biochemical data for the development of novel antibiotic drugs. In this review, we introduce diverse structural and biochemical studies on M. tuberculosis proteins determined using NMR spectroscopy.
Highlights
Mycobacterium tuberculosis quickly became a global epidemic in the 18th century and continues to threaten global health in the 21st century
We introduce the diverse structural and biochemical studies of M. tuberculosis proteins based on nuclear magnetic resonance (NMR) experiments
Valuable findings based on chemical shift perturbation and ligand-binding studies reveal information regarding biophysical mechanisms and dynamics of target proteins, which can be applied for anti-tuberculosis drug discovery
Summary
Mycobacterium tuberculosis quickly became a global epidemic in the 18th century and continues to threaten global health in the 21st century. In one gene cluster of M. tuberculosis, 122 genes are related to more than three essential metabolic pathways; among them, 55 genes are predicted to be indispensable for survival and the maintenance of M. tuberculosis [8] Based on these bioinformatics data, proteins in M. tuberculosis contain various novel therapeutic targets. Considering the clinical importance of M. tuberculosis, the protein data bank (PDB) contains a total of 2067 structures of the proteins alone and in complex with binding partners (chemicals or proteins) from this bacterium. Valuable findings based on chemical shift perturbation and ligand-binding studies reveal information regarding biophysical mechanisms and dynamics of target proteins, which can be applied for anti-tuberculosis drug discovery
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