7TK6

Yeast ATP synthase State 1catalytic(a) with 10 mM ATP backbone model

This is a non-PDB format compatible entry.

Summary for 7TK6

• Entry DOI: 10.2210/pdb7tk6/pdb
• EMDB information: 25958
• Descriptor: ATP synthase subunit 9, mitochondrial, ATP synthase subunit d, ATP synthase subunit f, ... (14 entities in total)
• Functional Keywords: f1-atpase, atp synthase, hydrolase, nanomotor, complex
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 27
• Total formula weight: 573259.05

Authors

Guo, H.,Rubinstein, J.L. (deposition date: 2022-01-17, release date: 2022-04-20, Last modification date: 2024-02-21)

Primary citation

Guo, H.,Rubinstein, J.L.
Structure of ATP synthase under strain during catalysis.
Nat Commun, 13:2232-2232, 2022

PubMed Abstract: ATP synthases are macromolecular machines consisting of an ATP-hydrolysis-driven F motor and a proton-translocation-driven F motor. The F and F motors oppose each other's action on a shared rotor subcomplex and are held stationary relative to each other by a peripheral stalk. Structures of resting mitochondrial ATP synthases revealed a left-handed curvature of the peripheral stalk even though rotation of the rotor, driven by either ATP hydrolysis in F or proton translocation through F, would apply a right-handed bending force to the stalk. We used cryoEM to image yeast mitochondrial ATP synthase under strain during ATP-hydrolysis-driven rotary catalysis, revealing a large deformation of the peripheral stalk. The structures show how the peripheral stalk opposes the bending force and suggests that during ATP synthesis proton translocation causes accumulation of strain in the stalk, which relaxes by driving the relative rotation of the rotor through six sub-steps within F, leading to catalysis.

PubMed: 35468906
DOI: 10.1038/s41467-022-29893-2

Experimental method

ELECTRON MICROSCOPY (6.5 Å)