Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii .

Autor: Demmer JK; Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK., Phillips BP; Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK., Uhrig OL; Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK., Filloux A; MRC Centre for Molecular Bacteriology and Infection, Department of Life Sciences, Imperial College London, London SW7 2AZ, UK., Allsopp LP; MRC Centre for Molecular Bacteriology and Infection, Department of Life Sciences, Imperial College London, London SW7 2AZ, UK.; National Heart and Lung Institute, Imperial College, London, UK., Bublitz M; Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK., Meier T; Department of Life Sciences, Imperial College London, Exhibition Road, London SW7 2AZ, UK.; Private University in the Principality of Liechtenstein, Triesen, Liechtenstein.
Jazyk: angličtina
Zdroj: Science advances [Sci Adv] 2022 Feb 18; Vol. 8 (7), pp. eabl5966. Date of Electronic Publication: 2022 Feb 16.
DOI: 10.1126/sciadv.abl5966
Abstrakt: 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 F 1 F o -adenosine 5'-triphosphate (ATP) synthase from A. baumannii in three distinct conformational states. The nucleotide-converting F 1 subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded F o 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.
Databáze: MEDLINE
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