Journal:Acta Cryst F:S2053230X19004618

Novel T9 loop interaction of Filamenting Temperature-sensitive mutant Z from Mycobacterium tuberculosis

E. O. Lazo, J. Jakoncic, S. RoyChowdhury, D. Awasthi, I. Ojima ^[1]

Molecular Tour
As of 2017, tuberculosis has infected 1.7 billion people (23% of the world's population) and has caused 10 million deaths. Mycobacterium tuberculosis (Mtb) is quickly evolving, and new strains are classified as multi-drug resistant. Thus, the development and discovery of new drugs to combat Mtb is vital to combat the drug-resistant strains. Filamenting temperature-sensitive mutant Z (FtsZ), an important protein involved in cell-division is key for the survival of Mtb. Here, we have solved the crystal structure of MtbFtsZ that exhibit an inter-subunit that plays a biological role in the GTPase activity of MtbFtsZ and have elucidated a novel conformation, involving the T9 loop and the nucleotide binding pocket that breaks up the GTPase active site. This novel conformation can serve as basis for the development of the novel drugs to combat tuberculosis.

References

1. ↑ Lazo EO, Jakoncic J, RoyChowdhury S, Awasthi D, Ojima I. Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis. Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):359-367. doi:, 10.1107/S2053230X19004618. Epub 2019 Apr 24. PMID:31045565 doi:http://dx.doi.org/10.1107/S2053230X19004618