EMD-4827
Cryo-EM structure of Polytomella F-ATP synthase, Rotary substate 1D, composite map
EMD-4827
Single-particle4.0 Å
Deposition: 12/04/2019Map released: 03/07/2019
Last modified: 22/05/2024
Sample Organism:
Polytomella sp. Pringsheim 198.80
Sample: Mitochondrial F-ATP synthase dimer from Polytomella sp. Pringsheim 198.80
Fitted models: 6rdq (Avg. Q-score: 0.404)
Raw data: EMPIAR-10375
Deposition Authors: Murphy BJ
,
Klusch N
Sample: Mitochondrial F-ATP synthase dimer from Polytomella sp. Pringsheim 198.80
Fitted models: 6rdq (Avg. Q-score: 0.404)
Raw data: EMPIAR-10375
Deposition Authors: Murphy BJ
,
Klusch N
Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Abstract:
F1Fo-adenosine triphosphate (ATP) synthases make the energy of the proton-motive force available for energy-consuming processes in the cell. We determined the single-particle cryo-electron microscopy structure of active dimeric ATP synthase from mitochondria of Polytomella sp. at a resolution of 2.7 to 2.8 angstroms. Separation of 13 well-defined rotary substates by three-dimensional classification provides a detailed picture of the molecular motions that accompany c-ring rotation and result in ATP synthesis. Crucially, the F1 head rotates along with the central stalk and c-ring rotor for the first ~30° of each 120° primary rotary step to facilitate flexible coupling of the stoichiometrically mismatched F1 and Fo subcomplexes. Flexibility is mediated primarily by the interdomain hinge of the conserved OSCP subunit. A conserved metal ion in the proton access channel may synchronize c-ring protonation with rotation.
F1Fo-adenosine triphosphate (ATP) synthases make the energy of the proton-motive force available for energy-consuming processes in the cell. We determined the single-particle cryo-electron microscopy structure of active dimeric ATP synthase from mitochondria of Polytomella sp. at a resolution of 2.7 to 2.8 angstroms. Separation of 13 well-defined rotary substates by three-dimensional classification provides a detailed picture of the molecular motions that accompany c-ring rotation and result in ATP synthesis. Crucially, the F1 head rotates along with the central stalk and c-ring rotor for the first ~30° of each 120° primary rotary step to facilitate flexible coupling of the stoichiometrically mismatched F1 and Fo subcomplexes. Flexibility is mediated primarily by the interdomain hinge of the conserved OSCP subunit. A conserved metal ion in the proton access channel may synchronize c-ring protonation with rotation.