Article
Structural diversity in twin-arginine signal peptide-binding proteins.
Proceedings of the National Academy of Sciences of the United States of America - 2 Oct 2007
Maillard Julien, Spronk Chris A E M, Buchanan Grant, Lyall Verity, Richardson David J, Palmer Tracy, Vuister Geerten W, Sargent Frank
Abstract excerpt
The twin-arginine transport (Tat) system is dedicated to the translocation of folded proteins across the bacterial cytoplasmic membrane. Proteins are targeted to the Tat system by signal peptides containing a twin-arginine motif. In Escherichia coli, many Tat substrates bind redox-active cofactors in the cytoplasm before transport. Coordination of cofactor insertion with protein export involves a "Tat...
Topics
- Arginine
- Binding Sites
- Carrier Proteins
- Escherichia coli
- Escherichia coli Proteins
- Genetic Variation
- Membrane Transport Proteins
- Nitrate Reductase
- Oxidation-Reduction
- Protein Binding
- Protein Sorting Signals
- Signal Transduction
- Substrate Specificity