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TitleCryo-EM structures of the autoinhibited ATP synthase in three rotational states.
Journal, issue, pagesElife, Vol. 5, Year 2016
Publish dateDec 21, 2016
AuthorsMeghna Sobti / Callum Smits / Andrew Sw Wong / Robert Ishmukhametov / Daniela Stock / Sara Sandin / Alastair G Stewart /
PubMed AbstractA molecular model that provides a framework for interpreting the wealth of functional information obtained on the F-ATP synthase has been generated using cryo-electron microscopy. Three different ...A molecular model that provides a framework for interpreting the wealth of functional information obtained on the F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk's ε subunit in an extended autoinhibitory conformation in all three states. The F motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire length of the complex, revealing the F attachment points and a coiled-coil that bifurcates toward the membrane with its helices separating to embrace subunit from two sides.
External linksElife / PubMed:28001127 / PubMed Central
MethodsEM (single particle)
Resolution6.9 - 8.53 Å
Structure data

EMDB-8357, PDB-5t4o:
Autoinhibited E. coli ATP synthase state 1
Method: EM (single particle) / Resolution: 6.9 Å

EMDB-8358, PDB-5t4p:
Autoinhibited E. coli ATP synthase state 2
Method: EM (single particle) / Resolution: 7.77 Å

EMDB-8359, PDB-5t4q:
Autoinhibited E. coli ATP synthase state 3
Method: EM (single particle) / Resolution: 8.53 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

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

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / ATP synthase / ATPase / rotary motor / membrane protein

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