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TitleIn situ structure and rotary states of mitochondrial ATP synthase in whole cells.
Journal, issue, pagesScience, Vol. 385, Issue 6713, Page 1086-1090, Year 2024
Publish dateSep 6, 2024
AuthorsLea Dietrich / Ahmed-Noor A Agip / Christina Kunz / Andre Schwarz / Werner Kühlbrandt /
PubMed AbstractCells 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 ...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.
External linksScience / PubMed:39236170
MethodsEM (subtomogram averaging)
Resolution5.6 - 6.9 Å
Structure data

19999

9evd

EMDB-19999, PDB-9evd:
In situ structure of the peripheral stalk of the mitochondrial ATPsynthase in whole Polytomella cells
Method: EM (subtomogram averaging) / Resolution: 5.6 Å

EMDB-50000: In situ structure of mitochondrial ATPsynthase in whole Polytomella cells
Method: EM (subtomogram averaging) / Resolution: 6.8 Å

EMDB-50001: Structure of the peripheral stalk of the Polytomella ATPsynthase dimer in whole cells
Method: EM (subtomogram averaging) / Resolution: 6.9 Å

Source
  • Polytomella (plant)
  • polytomella sp. pringsheim 198.80 (plant)
KeywordsMEMBRANE PROTEIN / ATP synthesis / in situ / OXPHOS

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