6rep | pdb_00006rep

Cryo-EM structure of Polytomella F-ATP synthase, Primary rotary state 3, composite map

spinqualitylabelsall models 6rep, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rep is a 30 chain structure with sequence from Polytomella sp. pringsheim 198.80. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, ATP, MG, ZN Activity: H(+)-transporting two-sector ATPase, with EC number 7.1.2.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [A0ZW40_9CHLO] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003551] [A0ZW41_9CHLO] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003553] Publication Abstract from PubMed 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 degrees of each 120 degrees 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. Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling.,Murphy BJ, Klusch N, Langer J, Mills DJ, Yildiz O, Kuhlbrandt W Science. 2019 Jun 21;364(6446). pii: 364/6446/eaaw9128. doi:, 10.1126/science.aaw9128. Epub 2019 Jun 20. PMID:31221832 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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