8DBT

E. coli ATP synthase imaged in 10mM MgATP State2 "down

This is a non-PDB format compatible entry.

Summary for 8DBT

• Entry DOI: 10.2210/pdb8dbt/pdb
• Related: 8DBP 8DBQ 8DBR 8DBS 8DBU 8DBV 8DBW
• EMDB information: 27296 27297 27298 27299 27300 27301 27302 27303 27304 27305 27306 27307 27308 27309 27310 27311 27312 27313 27314 27315
• Descriptor: ATP synthase subunit alpha, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (11 entities in total)
• Functional Keywords: energy, atp hyrolysis, atp synthesis, motor, membrane protein, cryoem
• Biological source: Escherichia coli; More
• Total number of polymer chains: 22
• Total formula weight: 536869.43

Authors

Sobti, M.,Stewart, A.G. (deposition date: 2022-06-14, release date: 2023-01-25, Last modification date: 2024-06-12)

Primary citation

Sobti, M.,Zeng, Y.C.,Walshe, J.L.,Brown, S.H.J.,Ishmukhametov, R.,Stewart, A.G.
Changes within the central stalk of E. coli F 1 F o ATP synthase observed after addition of ATP.
Commun Biol, 6:26-26, 2023

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 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.

PubMed: 36631659
DOI: 10.1038/s42003-023-04414-z

Experimental method

ELECTRON MICROSCOPY (3.1 Å)