Recent research published in Communications Biology marks an advance in structural biology by enhancing understanding of protein regulation mechanisms in Mycobacterium tuberculosis (Mtb), a global health threat. The team led by the University of Melbourne combined several advanced techniques at the Australian Synchrotron and the National Deuteration Facility to reveal the hidden allosteric mechanism that activates a key enzyme, ICL2.
The study opens a target pathway to treat drug-resistant TB with modulators that can interfere with the enzyme’s “on switch.” Traditional drugs often targeted the enzyme’s active site, which is difficult to block effectively.
However, ICL2 is unique to mycobacteria and is essential for the survival of the TB bacterium during infection, especially when it is starved of sugar and forced to live on fats.






