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The **ATP synthase subunit c** in *Mycobacterium tuberculosis* is a critical component of the membrane-embedded Fo sector of the F-type ATP synthase complex, responsible for translocating protons across the bacterial membrane and driving the synthesis of ATP from ADP[7][5][4]. This target is essential for mycobacterial survival and energy metabolism. Bedaquiline, a diarylquinoline antibiotic, binds specifically to the c subunit, blocking its rotary mechanism and thus ATP generation—a mechanism unique to mycobacteria that provides selectivity over human ATP synthases. The essential nature of this subunit in *M. tuberculosis* and its unique structural features compared to eukaryotic homologs establish it as a validated and druggable target for tuberculosis therapeutics[4][5][7].
Inhibition of proton translocation by binding to the c subunit, thereby blocking ATP synthesis and leading to energy depletion in Mycobacterium tuberculosis[4][5]
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