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Title | Structure of ATP synthase from ESKAPE pathogen . |
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Journal, issue, pages | Sci Adv, Vol. 8, Issue 7, Page eabl5966, Year 2022 |
Publish date | Feb 18, 2022 |
Authors | Julius K Demmer / Ben P Phillips / O Lisa Uhrig / Alain Filloux / Luke P Allsopp / Maike Bublitz / Thomas Meier / |
PubMed Abstract | The global spread of multidrug-resistant infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the FF-adenosine 5'-triphosphate ...The global spread of multidrug-resistant infections urgently calls for the identification of novel drug targets. We solved the electron cryo-microscopy structure of the FF-adenosine 5'-triphosphate (ATP) synthase from in three distinct conformational states. The nucleotide-converting F subcomplex reveals a specific self-inhibition mechanism, which supports a unidirectional ratchet mechanism to avoid wasteful ATP consumption. In the membrane-embedded F 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. |
External links | Sci Adv / PubMed:35171679 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.1 - 4.6 Å |
Structure data | EMDB-13174, PDB-7p2y: EMDB-13181, PDB-7p3n: EMDB-13186, PDB-7p3w: |
Chemicals | ChemComp-ATP: ChemComp-MG: ChemComp-ADP: ChemComp-PO4: ChemComp-HOH: |
Source |
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Keywords | MEMBRANE PROTEIN / ATP synthase / ESKAPE / Rotary ATP synthase / F1Fo / peptidisc / bioenergetics / IMP / multi-drug resistance / pathogenic |