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7TJV

Yeast ATP synthase F1 region State 1catalytic(a) with 10 mM ATP

This is a non-PDB format compatible entry.
Summary for 7TJV
Entry DOI10.2210/pdb7tjv/pdb
EMDB information25933
DescriptorATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (6 entities in total)
Functional Keywordsf1-atpase, atp synthase, hydrolase, nanomotor, complex
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains7
Total formula weight351800.06
Authors
Guo, H.,Rubinstein, J.L. (deposition date: 2022-01-17, release date: 2022-04-20, Last modification date: 2024-02-21)
Primary citationGuo, H.,Rubinstein, J.L.
Structure of ATP synthase under strain during catalysis.
Nat Commun, 13:2232-2232, 2022
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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