Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.

@article{Bulieris2003FoldingAI,
  title={Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide.},
  author={Paula V Bulieris and Susanne Behrens and Otto Holst and J{\"o}rg H. Kleinschmidt},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 11},
  pages={9092-9}
}
We have studied the folding pathway of a beta-barrel membrane protein using outer membrane protein A (OmpA) of Escherichia coli as an example. The deletion of the gene of periplasmic Skp impairs the assembly of outer membrane proteins of bacteria. We investigated how Skp facilitates the insertion and folding of completely unfolded OmpA into phospholipid membranes and which are the biochemical and biophysical requirements of a possible Skp-assisted folding pathway. In refolding experiments, Skp… CONTINUE READING

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