Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.

@article{Banci2010MolecularCF,
  title={Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import.},
  author={Lucia Banci and Ivano Bertini and Chiara Cefaro and Lucia Cenacchi and Simone Ciofi-Baffoni and Isabella C. Felli and Angelo Gallo and Leonardo Gonnelli and Enrico Luchinat and Dionisia P. Sideris and Kostas Tokatlidis},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 47},
  pages={20190-5}
}
Several proteins of the mitochondrial intermembrane space are targeted by internal targeting signals. A class of such proteins with α-helical hairpin structure bridged by two intramolecular disulfides is trapped by a Mia40-dependent oxidative process. Here, we describe the oxidative folding mechanism underpinning this process by an exhaustive structural characterization of the protein in all stages and as a complex with Mia40. Two consecutive induced folding steps are at the basis of the… CONTINUE READING

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