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-Structure paper
Title | Cryo-EM structures of the autoinhibited ATP synthase in three rotational states. |
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Journal, issue, pages | Elife, Vol. 5, Year 2016 |
Publish date | Dec 21, 2016 |
Authors | Meghna Sobti / Callum Smits / Andrew Sw Wong / Robert Ishmukhametov / Daniela Stock / Sara Sandin / Alastair G Stewart / |
PubMed Abstract | 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 ...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 links | Elife / PubMed:28001127 / PubMed Central |
Methods | EM (single particle) |
Resolution | 6.9 - 8.53 Å |
Structure data | EMDB-8357, PDB-5t4o: |
Chemicals | ChemComp-ATP: ChemComp-ADP: |
Source |
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Keywords | HYDROLASE / ATP synthase / ATPase / rotary motor / membrane protein |