Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism

@article{Walther2013FoldingAS,
  title={Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism},
  author={Torsten H. Walther and Christina Gottselig and Stephan L. Grage and Moritz Wolf and Attilio Vittorio Vargiu and Marco J. Klein and Stefanie Vollmer and Sebastian Prock and Mareike Hartmann and Sergiy Afonin and Eva Stockwald and Hartmut Heinzmann and Olga V. Nolandt and Wolfgang Wenzel and Paolo Ruggerone and Anne S Ulrich},
  journal={Cell},
  year={2013},
  volume={152},
  pages={316-326}
}
We propose a concept for the folding and self-assembly of the pore-forming TatA complex from the Twin-arginine translocase and of other membrane proteins based on electrostatic "charge zippers." Each subunit of TatA consists of a transmembrane segment, an amphiphilic helix (APH), and a C-terminal densely charged region (DCR). The sequence of charges in the DCR is complementary to the charge pattern on the APH, suggesting that the protein can be "zipped up" by a ladder of seven salt bridges. The… CONTINUE READING