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Stealth switch in tuberculosis enzyme could open route to drug-resistant treatment

phys.org·Australian Nuclear Science and Technology Organisation (ANSTO)·about 1 month ago
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Communications Biology (2026). DOI: 10.1038/s42003-026-09821-6, Creative Commons 4.0 license ."> Structure of Mtb ICL2, which forms a homotetramer. Each monomer is indicated by a different colour with one monomer coloured according to the three features present in each monomer. The active site and acetyl-CoA-binding site are also labelled. Credit: Communications Biology (2026). DOI: 10.1038/s42003-026-09821-6, Creative Commons 4.0 license . 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.…

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