Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM reveals transition states of the Acinetobacter baumannii F-ATPase rotary subunits γ and ε, unveiling novel compound targets.
Journal, issue, pages	FASEB J, Vol. 38, Issue 20, Page e70131, Year 2024
Publish date	Oct 28, 2024
Authors	Khoa Cong Minh Le / Chui Fann Wong / Volker Müller / Gerhard Grüber /
PubMed Abstract	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 ...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 links	FASEB J / PubMed:39467208
Methods	EM (single particle)
Resolution	2.89 - 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 moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION
Source	acinetobacter baumannii ab5075 (bacteria)
Keywords	HYDROLASE / ATP hydrolysis / F1-ATPase