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Structure of ATP synthase from ESKAPE pathogen Acinetobacter baumannii.


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.

SUBMITTER: Demmer JK 

PROVIDER: S-EPMC8849298 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature

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Structure of ATP synthase from ESKAPE pathogen <i>Acinetobacter baumannii</i>.

Demmer Julius K JK   Phillips Ben P BP   Uhrig O Lisa OL   Filloux Alain A   Allsopp Luke P LP   Bublitz Maike M   Meier Thomas T  

Science advances 20220216 7


The global spread of multidrug-resistant <i>Acinetobacter baumannii</i> infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the F<sub>1</sub>F<sub>o</sub>-adenosine 5'-triphosphate (ATP) synthase from <i>A. baumannii</i> in three distinct conformational states. The nucleotide-converting F<sub>1</sub> subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful A  ...[more]

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