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	Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy.
Journal, issue, pages	Nat Commun, Year 2025
Publish date	Dec 9, 2025
Authors	Meghna Sobti / Adam P Gunn / Simon H J Brown / Lauren Zavan / Vesper M Fraunfelter / Amanda L Wolfe / Christopher A McDevitt / P Ryan Steed / Alastair G Stewart /
PubMed Abstract	FF ATP synthase is the ubiquitous enzyme that synthesizes cellular ATP by coupling proton-motive force with rotational catalysis. Structural differences between prokaryotic and eukaryotic ATP ...FF ATP synthase is the ubiquitous enzyme that synthesizes cellular ATP by coupling proton-motive force with rotational catalysis. Structural differences between prokaryotic and eukaryotic ATP synthases offer potential targets for antimicrobial development. Here, we present the 2.0-2.4 Å resolution cryo-electron microscopy structures of the ATP synthase from Pseudomonas aeruginosa, an opportunistic bacterial pathogen capable of causing serious infections in humans. Our structures identify two distinctive features of this species' enzyme: a distinct binding site for the inhibitory ε subunit, and a coordinated metal ion capping the cytoplasmic proton channel. Lower-resolution maps of the enzyme following incubation with MgATP showed conformational rearrangements of the ε subunit during activation. Visualization of bound water molecules in the periplasmic half-channel supports a Grotthuss proton-transfer mechanism. Focused classification of the F motor resolves distinct ~11° sub-steps in the c-ring, corresponding to protonation and deprotonation events. Functional analyses show that modifications to either the ε subunit or the metal binding site influence ATP synthesis and hydrolysis. Mass spectrometry analyses suggests that the physiological metal within the complex is zinc. Collectively, these findings define structural features of P. aeruginosa ATP synthase that could serve as targets for antimicrobial therapeutics.
External links	Nat Commun / PubMed:41366214
Methods	EM (single particle)
Resolution	2.0 - 3.57 Å
Structure data	49999 9o19 EMDB-49999, PDB-9o19: Pseudomonas aeruginosa ATPase State1 Method: EM (single particle) / Resolution: 2.0 Å 70000 9o1a EMDB-70000, PDB-9o1a: Pseudomonas aeruginosa ATPase State1 F1Fo focused Method: EM (single particle) / Resolution: 2.77 Å 70001 9o1b EMDB-70001, PDB-9o1b: Pseudomonas aeruginosa ATPase State1 Fo focused Method: EM (single particle) / Resolution: 2.37 Å 70002 9o1c EMDB-70002, PDB-9o1c: Pseudomonas aeruginosa ATPase State2 Method: EM (single particle) / Resolution: 2.05 Å 70003 9o1d EMDB-70003, PDB-9o1d: Pseudomonas aeruginosa ATPase State2a F1Fo focused Method: EM (single particle) / Resolution: 3.23 Å 70004 9o1e EMDB-70004, PDB-9o1e: Pseudomonas aeruginosa ATPase State2a Fo focused Method: EM (single particle) / Resolution: 2.59 Å 70005 9o1f EMDB-70005, PDB-9o1f: Pseudomonas aeruginosa ATPase State2b F1Fo focused Method: EM (single particle) / Resolution: 2.76 Å 70006 9o1g EMDB-70006, PDB-9o1g: Pseudomonas aeruginosa ATPase State2b Fo focused Method: EM (single particle) / Resolution: 2.66 Å 70007 9o1h EMDB-70007, PDB-9o1h: Pseudomonas aeruginosa ATPase State3 Method: EM (single particle) / Resolution: 2.17 Å 70009 9o1j EMDB-70009, PDB-9o1j: Pseudomonas aeruginosa ATPase State3 F1Fo focused Method: EM (single particle) / Resolution: 3.02 Å 70010 9o1k EMDB-70010, PDB-9o1k: Pseudomonas aeruginosa ATPase State3 Fo focused Method: EM (single particle) / Resolution: 3.01 Å EMDB-71967: Pseudomonas aeruginosa ATPase State2 with 10mM MgATP "Up" Method: EM (single particle) / Resolution: 3.37 Å EMDB-71968: Pseudomonas aeruginosa ATPase State2 with 10mM MgATP "Down" Method: EM (single particle) / Resolution: 3.57 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 ChemComp-HOH: WATER ChemComp-ZN: Unknown entry
Source	pseudomonas aeruginosa (bacteria)
Keywords	ELECTRON TRANSPORT / ATPase / energy / Cryo-EM / single particle