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TitleThe molecular structure of an axle-less F-ATPase.
Journal, issue, pagesBiochim Biophys Acta Bioenerg, Vol. 1866, Issue 1, Page 149521, Year 2024
Publish dateOct 18, 2024
AuthorsEmily J Furlong / Ian-Blaine P Reininger-Chatzigiannakis / Yi C Zeng / Simon H J Brown / Meghna Sobti / Alastair G Stewart /
PubMed AbstractFF ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F-ATPase catalytic cores can hydrolyse ATP, passing through a series of ...FF ATP synthase is a molecular rotary motor that can generate ATP using a transmembrane proton motive force. Isolated F-ATPase catalytic cores can hydrolyse ATP, passing through a series of conformational states involving rotation of the central γ rotor subunit and the opening and closing of the catalytic β subunits. Cooperativity in F-ATPase has long thought to be conferred through the γ subunit, with three key interaction sites between the γ and β subunits being identified. Single molecule studies have demonstrated that the F complexes lacking the γ axle still "rotate" and hydrolyse ATP, but with less efficiency. We solved the cryogenic electron microscopy structure of an axle-less Bacillus sp. PS3 F-ATPase. The unexpected binding-dwell conformation of the structure in combination with the observed lack of interactions between the axle-less γ and the open β subunit suggests that the complete γ subunit is important for coordinating efficient ATP binding of F-ATPase.
External linksBiochim Biophys Acta Bioenerg / PubMed:39428050
MethodsEM (single particle)
Resolution3.0 - 3.72 Å
Structure data

41811

8u1h

EMDB-41811, PDB-8u1h:
Axle-less Bacillus sp. PS3 F1 ATPase mutant
Method: EM (single particle) / Resolution: 3.0 Å

43903

9avj

EMDB-43903, PDB-9avj:
PS3 F1 ATPase Wild type
Method: EM (single particle) / Resolution: 3.72 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-PO4:
PHOSPHATE ION

Source
  • bacillus sp. ps3 (bacteria)
KeywordsHYDROLASE / ATPase / ATP synthase / MEMBRANE PROTEIN / electron transfer / ATP hydrolysis

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