9EVD
In situ structure of the peripheral stalk of the mitochondrial ATPsynthase in whole Polytomella cells
Summary for 9EVD
| Entry DOI | 10.2210/pdb9evd/pdb |
| EMDB information | 19999 |
| Descriptor | ASA-10: Polytomella F-ATP synthase associated subunit 10, ATP synthase associated protein ASA1, Mitochondrial F1F0 ATP synthase associated 32 kDa protein, ... (9 entities in total) |
| Functional Keywords | atp synthesis, in situ, oxphos, membrane protein |
| Biological source | Polytomella sp. Pringsheim 198.80 More |
| Total number of polymer chains | 9 |
| Total formula weight | 218411.41 |
| Authors | |
| Primary citation | Dietrich, L.,Agip, A.A.,Kunz, C.,Schwarz, A.,Kuhlbrandt, W. In situ structure and rotary states of mitochondrial ATP synthase in whole Polytomella cells. Science, 385:1086-1090, 2024 Cited by PubMed Abstract: 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 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 head. The 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. PubMed: 39236170DOI: 10.1126/science.adp4640 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.6 Å) |
Structure validation
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