Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases

@article{Sielaff2019StructuralAA,
  title={Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases},
  author={Hendrik Sielaff and Seiga Yanagisawa and Wayne D. Frasch and Wolfgang Junge and Michael B{\"o}rsch},
  journal={Molecules},
  year={2019},
  volume={24}
}
F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F1 domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)3δab2. Subunits c10 or (αβ)3 alone are rotationally symmetric. However, symmetry is broken by the b2 homodimer, which together with subunit δa, forms a single eccentric stalk connecting the membrane embedded FO domain with the soluble F1 domain, and the central rotating and curved stalk composed of subunit γε. Although… 

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