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	Changes within the central stalk of E. coli FF ATP synthase observed after addition of ATP.
Journal, issue, pages	Commun Biol, Vol. 6, Issue 1, Page 26, Year 2023
Publish date	Jan 11, 2023
Authors	Meghna Sobti / Yi C Zeng / James L Walshe / Simon H J Brown / Robert Ishmukhametov / Alastair G Stewart /
PubMed Abstract	FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to ...FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to catalyze ATP production, with flexible F/F coupling required for efficient catalysis. FF ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli FF ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F motor. This highlights the importance of the central rotor for flexible coupling of the F and F motors and provides further insight into the regulatory mechanism mediated by subunit ε.
External links	Commun Biol / PubMed:36631659 / PubMed Central
Methods	EM (single particle)
Resolution	2.7 - 7.8 Å
Structure data	EMDB-27296: E. coli ATP synthase imaged in 10mM MgATP State1 Method: EM (single particle) / Resolution: 3.0 Å 27297 8dbp EMDB-27297, PDB-8dbp: E. coli ATP synthase imaged in 10mM MgATP State1 "half-up Method: EM (single particle) / Resolution: 3.6 Å 27298 8dbq EMDB-27298: E.coli ATP synthase imaged in 10mM MgATP State1 "half-up" Fo classified PDB-8dbq: E. coli ATP synthase imaged in 10mM MgATP State1 "half-up" Fo classified Method: EM (single particle) / Resolution: 4.0 Å EMDB-27299: E. coli ATP synthase imaged in 10mM MgATP State 1 "half-up" Fo refine Method: EM (single particle) / Resolution: 7.4 Å EMDB-27300: E. coli ATP synthase imaged in 10mM MgATP State1 "down" Method: EM (single particle) / Resolution: 7.2 Å EMDB-27301: E. coli ATP synthase imaged in 10mM MgATP State 1 "down" Fo classified Method: EM (single particle) / Resolution: 7.8 Å EMDB-27302: E. coli ATP synthase imaged in 10mM MgATP State2 Method: EM (single particle) / Resolution: 2.7 Å 27303 8dbr EMDB-27303, PDB-8dbr: E. coli ATP synthase imaged in 10mM MgATP State2 "half-up Method: EM (single particle) / Resolution: 3.2 Å 27304 8dbs EMDB-27304, PDB-8dbs: E. coli ATP synthase imaged in 10mM MgATP State2 "half-up" Fo classified Method: EM (single particle) / Resolution: 3.5 Å EMDB-27305: E. coli ATP synthase imaged in 10mM MgATP State2 "half-up" Fo refine Method: EM (single particle) / Resolution: 7.0 Å 27306 8dbt EMDB-27306, PDB-8dbt: E. coli ATP synthase imaged in 10mM MgATP State2 "down Method: EM (single particle) / Resolution: 3.1 Å 27307 8dbu EMDB-27307, PDB-8dbu: E. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo classified Method: EM (single particle) / Resolution: 3.4 Å EMDB-27308: E. coli ATP synthase imaged in 10mM MgATP State2 "down" Fo refine Method: EM (single particle) / Resolution: 7.2 Å EMDB-27309: E. coli ATP synthase imaged in 10mM MgATP State3 Method: EM (single particle) / Resolution: 3.0 Å 27310 8dbv EMDB-27310, PDB-8dbv: E. coli ATP synthase imaged in 10mM MgATP State3 "down Method: EM (single particle) / Resolution: 3.7 Å 27311 8dbw EMDB-27311, PDB-8dbw: E. coli ATP synthase imaged in 10mM MgATP State3 "down" Fo classified Method: EM (single particle) / Resolution: 4.1 Å EMDB-27312: E. coli ATP synthase imaged in 10mM MgATP State3 "down" Fo refine Method: EM (single particle) / Resolution: 7.4 Å EMDB-27313: E. coli ATP synthase epsilon helix1 deletion mutant imaged in 10mM MgATP State1 Method: EM (single particle) / Resolution: 4.0 Å EMDB-27314: E. coli ATP synthase epsilon helix1 deletion mutant imaged in 10mM MgATP State2 Method: EM (single particle) / Resolution: 3.3 Å EMDB-27315: E. coli ATP synthase epsilon helix1 deletion mutant imaged in 10mM MgATP State3 Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM
Source	escherichia coli (E. coli)
Keywords	MEMBRANE PROTEIN / Energy / ATP hyrolysis / ATP synthesis / Motor / cryoEM