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TitleStructure of ATP synthase from ESKAPE pathogen .
Journal, issue, pagesSci Adv, Vol. 8, Issue 7, Page eabl5966, Year 2022
Publish dateFeb 18, 2022
AuthorsJulius K Demmer / Ben P Phillips / O Lisa Uhrig / Alain Filloux / Luke P Allsopp / Maike Bublitz / Thomas Meier /
PubMed AbstractThe 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 linksSci Adv / PubMed:35171679 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 4.6 Å
Structure data

13174

7p2y

EMDB-13174, PDB-7p2y:
F1Fo-ATP synthase from Acinetobacter baumannii (state 1)
Method: EM (single particle) / Resolution: 3.1 Å

13181

7p3n

EMDB-13181, PDB-7p3n:
F1Fo-ATP synthase from Acinetobacter baumannii (state 2)
Method: EM (single particle) / Resolution: 4.6 Å

13186

7p3w

EMDB-13186, PDB-7p3w:
F1Fo-ATP synthase from Acinetobacter baumannii (state 3)
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377) (bacteria)
  • acinetobacter baumannii (strain atcc 17978 / cip 53.77 / lmg 1025 / ncdc kc755 / 5377) (bacteria)
  • acinetobacter baumannii atcc 17978 (bacteria)
KeywordsMEMBRANE PROTEIN / ATP synthase / ESKAPE / Rotary ATP synthase / F1Fo / peptidisc / bioenergetics / IMP / multi-drug resistance / pathogenic

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