New conformation of tuberculosis target protein FtsZ
What is it about?
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.
Why is it important?
This novel conformation can serve as basis for the development of the novel drugs to combat tuberculosis.