• Corpus ID: 2579641

Regulatory conformational changes of the epsilon subunit in single FRET-labeled FoF1-ATP synthase

@article{Duncan2014RegulatoryCC,
  title={Regulatory conformational changes of the epsilon subunit in single FRET-labeled FoF1-ATP synthase},
  author={Thomas M. Duncan and M. G. Dueser and Thomas Heitkamp and Duncan G. G. McMillan and Michael Boersch},
  journal={arXiv: Biomolecules},
  year={2014}
}
Subunit epsilon is an intrinsic regulator of the bacterial FoF1-ATP synthase, the ubiquitous membrane-embedded enzyme that utilizes a proton motive force in most organisms to synthesize adenosine triphosphate (ATP). The C-terminal domain of epsilon can extend into the central cavity formed by the alpha and beta subunits, as revealed by the recent X-ray structure of the F1 portion of the Escherichia coli enzyme. This insertion blocks the rotation of the central gamma subunit and, thereby… 

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