Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I

@inproceedings{Venditti2015LargeIR,
  title={Large interdomain rearrangement triggered by suppression of micro- to millisecond dynamics in bacterial Enzyme I},
  author={Vincenzo Venditti and Vitali Tugarinov and Charles D. Schwieters and Alexander Grishaev and G Marius Clore},
  booktitle={Nature communications},
  year={2015}
}
Enzyme I (EI), the first component of the bacterial phosphotransfer signal transduction system, undergoes one of the largest substrate-induced interdomain rearrangements documented to date. Here we characterize the perturbations generated by two small molecules, the natural substrate phosphoenolpyruvate and the inhibitor α-ketoglutarate, on the structure and dynamics of EI using NMR, small-angle X-ray scattering and biochemical techniques. The results indicate unambiguously that the open-to… CONTINUE READING
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