6RDD

Cryo-EM structure of Polytomella F-ATP synthase, Primary rotary state 2, monomer-masked refinement

Summary for 6RDD

• Entry DOI: 10.2210/pdb6rdd/pdb
• EMDB information: 4814
• Descriptor: ASA-10: Polytomella F-ATP synthase associated subunit 10, Mitochondrial ATP synthase subunit ASA9, Mitochondrial ATP synthase subunit 6, ... (15 entities in total)
• Functional Keywords: mitochondrial atp synthase dimer flexible coupling cryoem, proton transport
• Biological source: Polytomella sp. Pringsheim 198.80; More
• Total number of polymer chains: 13
• Total formula weight: 380890.99

Authors

Murphy, B.J.,Klusch, N.,Yildiz, O.,Kuhlbrandt, W. (deposition date: 2019-04-12, release date: 2019-07-03, Last modification date: 2024-05-22)

Primary citation

Murphy, B.J.,Klusch, N.,Langer, J.,Mills, D.J.,Yildiz, O.,Kuhlbrandt, W.
Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Science, 364:-, 2019

PubMed Abstract: FF-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 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 -ring rotation and result in ATP synthesis. Crucially, the F head rotates along with the central stalk and -ring rotor for the first ~30° of each 120° primary rotary step to facilitate flexible coupling of the stoichiometrically mismatched F and F 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 -ring protonation with rotation.

PubMed: 31221832
DOI: 10.1126/science.aaw9128

Experimental method

ELECTRON MICROSCOPY (3.2 Å)