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- W2069659439 abstract "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 length of the resulting hairpin matches the lipid bilayer thickness, hence a transmembrane pore could self-assemble via intra- and intermolecular salt bridges. The steric feasibility was rationalized by molecular dynamics simulations, and experimental evidence was obtained by monitoring the monomer-oligomer equilibrium of specific charge mutants. Similar charge zippers are proposed for other membrane-associated proteins, e.g., the biofilm-inducing peptide TisB, the human antimicrobial peptide dermcidin, and the pestiviral E(RNS) protein." @default.
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- W2069659439 date "2013-01-01" @default.
- W2069659439 modified "2023-09-27" @default.
- W2069659439 title "Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism" @default.
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- W2069659439 doi "https://doi.org/10.1016/j.cell.2012.12.017" @default.
- W2069659439 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23332763" @default.
- W2069659439 hasPublicationYear "2013" @default.
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