The global spread of multidrug-resistant Acinetobacter baumannii infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the F1Fo-adenosine 5′-triphosphate (ATP) synthase from A. baumannii in three distinct conformational states. The nucleotide-converting F1 subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded Fo complex, the structure shows unique structural adaptations along both the entry and exit pathways of the proton-conducting a-subunit. These features, absent in mitochondrial ATP synthases, represent attractive targets for the development of next-generation therapeutics that can act directly at the culmination of bioenergetics in this clinically relevant pathogen.
CITATION STYLE
Demmer, J. K., Phillips, B. P., Uhrig, O. L., Filloux, A., Allsopp, L. P., Bublitz, M., & Meier, T. (2022). Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii. Science Advances, 8(7). https://doi.org/10.1126/sciadv.abl5966
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