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TitleCryo-EM reveals transition states of the Acinetobacter baumannii F-ATPase rotary subunits γ and ε, unveiling novel compound targets.
Journal, issue, pagesFASEB J, Vol. 38, Issue 20, Page e70131, Year 2024
Publish dateOct 28, 2024
AuthorsKhoa Cong Minh Le / Chui Fann Wong / Volker Müller / Gerhard Grüber /
PubMed AbstractPriority 1: critical WHO pathogen Acinetobacter baumannii depends on ATP synthesis and ATP:ADP homeostasis and its bifunctional FF-ATP synthase. While synthesizing ATP, it regulates ATP cleavage by ...Priority 1: critical WHO pathogen Acinetobacter baumannii depends on ATP synthesis and ATP:ADP homeostasis and its bifunctional FF-ATP synthase. While synthesizing ATP, it regulates ATP cleavage by its inhibitory ε subunit to prevent wasteful ATP consumption. We determined cryo-electron microscopy structures of the ATPase active A. baumannii F-αßγε mutant in four distinct conformational states, revealing four transition states and structural transformation of the ε's C-terminal domain, forming the switch of an ATP hydrolysis off- and an ATP synthesis on-state based. These alterations go in concert with altered motions and interactions in the catalytic- and rotary subunits of this engine. These A. baumannii interacting sites provide novel pathogen-specific targets for inhibitors, with the aim of ATP depletion and/or ATP synthesis and growth inhibition. Furthermore, the presented diversity to other bacterial F-ATP synthases extends the view of structural elements regulating such a catalyst.
External linksFASEB J / PubMed:39467208 / PubMed Central
MethodsEM (single particle)
Resolution2.89 - 3.18 Å
Structure data

60117

8zi0

EMDB-60117, PDB-8zi0:
Cryo-EM reveals transition states of the Acinetobacter baumannii F1-ATPase rotary subunits gamma and epsilon and novel compound targets - Conformation 1
Method: EM (single particle) / Resolution: 3.18 Å

60118

8zi1

EMDB-60118, PDB-8zi1:
Cryo-EM reveals transition states of the Acinetobacter baumannii F1-ATPase rotary subunits gamma and epsilon and novel compound targets - Conformation 2
Method: EM (single particle) / Resolution: 2.92 Å

60119

8zi2

EMDB-60119, PDB-8zi2:
Cryo-EM reveals transition states of the Acinetobacter baumannii F1-ATPase rotary subunits gamma and epsilon and novel compound targets - Conformation 3
Method: EM (single particle) / Resolution: 2.99 Å

60120

8zi3

EMDB-60120, PDB-8zi3:
Cryo-EM reveals transition states of the Acinetobacter baumannii F1-ATPase rotary subunits gamma and epsilon and novel compound targets - Conformation 4
Method: EM (single particle) / Resolution: 2.89 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

Source
  • acinetobacter baumannii ab5075 (bacteria)
KeywordsHYDROLASE / ATP hydrolysis / F1-ATPase

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