Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii

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Abstract

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.

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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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