9evd

In situ structure of the peripheral stalk of the mitochondrial ATPsynthase in whole Polytomella cells

spinqualitylabelsall models 9evd, resolution 5.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9evd is a 9 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. Method: Electron Microscopy, Resolution 5.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A5H1ZR95_9CHLO Publication Abstract from PubMed Cells depend on a continuous supply of adenosine triphosphate (ATP), the universal energy currency. In mitochondria, ATP is produced by a series of redox reactions, whereby an electrochemical gradient is established across the inner mitochondrial membrane. The ATP synthase harnesses the energy of the gradient to generate ATP from adenosine diphosphate (ADP) and inorganic phosphate. We determined the structure of ATP synthase within mitochondria of the unicellular flagellate Polytomella by electron cryo-tomography and subtomogram averaging at up to 4.2-angstrom resolution, revealing six rotary positions of the central stalk, subclassified into 21 substates of the F(1) head. The Polytomella ATP synthase forms helical arrays with multiple adjacent rows defining the cristae ridges. The structure of ATP synthase under native operating conditions in the presence of a membrane potential represents a pivotal step toward the analysis of membrane protein complexes in situ. In situ structure and rotary states of mitochondrial ATP synthase in whole Polytomella cells.,Dietrich L, Agip AA, Kunz C, Schwarz A, Kuhlbrandt W Science. 2024 Sep 6;385(6713):1086-1090. doi: 10.1126/science.adp4640. Epub 2024 , Sep 5. PMID:39236170 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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