ATP synthase subunit c of Mycobacterium tuberculosis (AtpE)

ATP synthase subunit c of Mycobacterium tuberculosis (AtpE) is an integral membrane component of the F0 sector of the bacterial ATP synthase complex, forming part of the rotary c-ring that translocates protons across the membrane to drive the synthesis of ATP. It is essential for the energy metabolism of M. tuberculosis, enabling survival and persistence of the bacterium under both replicating and dormant conditions. Its unique structural features, which differ sufficiently from the human mitochondrial ATP synthase, allow selective targeting by the anti-tubercular drug bedaquiline. The high-affinity and specificity of drugs like bedaquiline for the mycobacterial c-ring make ATP synthase subunit c a central validated drug target in tuberculosis therapy, but the risk of drug resistance due to mutations must be considered[4][5][7].

Other names

AtpEc subunit of F1Fo-ATP synthaseF0 c subunitFo c subunit

Inhibition of proton translocation by binding to the c-ring, blocking rotation and thereby ATP production Destabilization of ATP synthase function, leading to energy collapse in the bacterium