Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB).

Tuberculosis is one of the deadliest diseases worldwide affecting approximately 10 million people in 2018. This classifies tuberculosis as epidemic in several countries and leads to an increasing number of multidrug-resistant strains. Thus, the development of new drugs is essential to effective treatments. A potential drug target is the ribose-5-phosphate isomerase, a ubiquitous enzyme important to nucleotide and cofactor biosynthesis. Here, we report the backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB) that has been performed by triple resonance sequential approach using a [13C, 15N, 2H]-labeled protein. This is the first ribose-5-phosphate isomerase, an enzyme previously classified as highly druggable, to be assigned. These data will be important to further screening studies to find inhibitors and determine their interaction with MtRpiB.

Backbone and side chain 1H, 15N and 13C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Mycobacterium tuberculosis.

FK506 Binding Proteins (FKBPs) are a family of highly conserved and important proteins that possess a peptidyl cis-trans isomerase (PPIases) domain. Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction with the immunosuppressive drugs FK506 and rapamycin. They inhibit calcineurin and mTOR complex, respectively, leading to parasite death by inhibiting cell proliferation through cytokinesis blockade being an important target to find new drugs. Tuberculosis is a disease that causes important impacts on public health worldwide. In this context, MtFKBP12 is a putative peptidyl prolyl cis-trans isomerase from Mycobacterium tuberculosis and here we report the NMR chemical shift assignment for 1H, 15N and 13C nuclei in the backbone and side chains of the MtFKBP12. This lays the foundation for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. We have found through the NMR spectrum that the protein is well folded with narrow peaks and almost none overlap in 15N-HSQC. Prediction of secondary structure using Talos-N server showed great similarity with other proteins from this family.