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	Structural basis of unisite catalysis of bacterial FF-ATPase.
Journal, issue, pages	PNAS Nexus, Vol. 1, Issue 3, Page pgac116, Year 2022
Publish date	Jul 11, 2022
Authors	Atsuki Nakano / Jun-Ichi Kishikawa / Atsuko Nakanishi / Kaoru Mitsuoka / Ken Yokoyama /
PubMed Abstract	Adenosine triphosphate (ATP) synthases (FF-ATPases) are crucial for all aerobic organisms. F, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the ...Adenosine triphosphate (ATP) synthases (FF-ATPases) are crucial for all aerobic organisms. F, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central rotor inside a cylinder made of in three different conformations (referred to as , , and ). In this study, we determined multiple cryo-electron microscopy structures of bacterial FF exposed to different reaction conditions. The structures of nucleotide-depleted FF indicate that the ε subunit directly forces to adopt a closed form independent of the nucleotide binding to . The structure of FF under conditions that permit only a single catalytic subunit per enzyme to bind ATP is referred to as unisite catalysis and reveals that ATP hydrolysis unexpectedly occurs on instead of , where ATP hydrolysis proceeds in the steady-state catalysis of FF. This indicates that the unisite catalysis of bacterial FF significantly differs from the kinetics of steady-state turnover with continuous rotation of the shaft.
External links	PNAS Nexus / PubMed:36741449 / PubMed Central
Methods	EM (single particle)
Resolution	2.6 - 4.5 Å
Structure data	33251 7xkh EMDB-33251, PDB-7xkh: Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, state1 Method: EM (single particle) / Resolution: 3.1 Å EMDB-33252: Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, , state2 Method: EM (single particle) / Resolution: 3.0 Å EMDB-33253: Nucleotide-depleted FoF1-ATPase from Bacillus PS3, state3 Method: EM (single particle) / Resolution: 3.7 Å 33258 7xko EMDB-33258, PDB-7xko: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,nucleotide depeleted Method: EM (single particle) / Resolution: 3.4 Å 33259 7xkp EMDB-33259, PDB-7xkp: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition Method: EM (single particle) / Resolution: 3.0 Å EMDB-33260: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition Method: EM (single particle) / Resolution: 3.2 Å EMDB-33261: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,nucleotide depleted Method: EM (single particle) / Resolution: 3.3 Å EMDB-33262: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,unisite condition Method: EM (single particle) / Resolution: 3.1 Å EMDB-33263: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state3,unisite condition Method: EM (single particle) / Resolution: 3.8 Å 33264 7xkq EMDB-33264, PDB-7xkq: F1 domain of FoF1-ATPase with the down form of epsilon subunit from Bacillus PS3 Method: EM (single particle) / Resolution: 3.3 Å 33265 7xkr EMDB-33265, PDB-7xkr: F1 domain of FoF1-ATPase with the up form of epsilon subunit from Bacillus PS3 Method: EM (single particle) / Resolution: 2.6 Å EMDB-33266: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state1 Method: EM (single particle) / Resolution: 2.9 Å EMDB-33267: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state2 Method: EM (single particle) / Resolution: 2.8 Å EMDB-33268: epsilon-inhibited FoF1-ATPase from Bacillus PS3 at saturated ATP-gamma-S condition, state3 Method: EM (single particle) / Resolution: 3.3 Å EMDB-33269: F1 domain of epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2',nucleotide depleted Method: EM (single particle) / Resolution: 4.5 Å EMDB-33277: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,nucleotide depleted Method: EM (single particle) / Resolution: 3.6 Å EMDB-33278: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1,unisite condition Method: EM (single particle) / Resolution: 3.2 Å EMDB-33279: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state1',unisite condition Method: EM (single particle) / Resolution: 3.4 Å EMDB-33280: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,nucleotide depleted Method: EM (single particle) / Resolution: 3.4 Å EMDB-33281: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2',nucleotide depleted Method: EM (single particle) / Resolution: 4.5 Å EMDB-33282: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state2,unisite condition Method: EM (single particle) / Resolution: 3.2 Å EMDB-33283: epsilon C-terminal domain deleted FoF1 from Bacillus PS3,state3,unisite condition Method: EM (single particle) / Resolution: 4.0 Å
Chemicals	ChemComp-PI: HYDROGENPHOSPHATE ION ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM
Source	bacillus sp. ps3 (bacteria)
Keywords	MOTOR PROTEIN / ATP synthase F1 ATPase FoF1