Tetrameric Charge-Zipper Assembly of the TisB Peptide in Membranes-Computer Simulation and Experiment.
Violetta SchneiderParvesh WadhwaniJohannes ReichertJochen BürckMarcus ElstnerAnne S UlrichTomáš KubařPublished in: The journal of physical chemistry. B (2019)
TisB is a short amphiphilic α-helical peptide from Escherichia coli that induces a breakdown of the pH gradient across the inner membrane when the bacteria are under stress and require to form persister cells to turn into a biofilm. A computational-experimental approach combining all-atom and coarse-grained molecular dynamics simulation with circular dichroism spectroscopy and gel electrophoresis was used to reveal its structure and oligomeric assembly in a phospholipid bilayer. TisB is found to be inserted upright in the membrane as a tetrameric bundle with a left-handed sense of supercoiling, best described as an antiparallel dimer-of-dimers. The tetramer is stabilized by means of a regular but dynamically interchanging pattern of salt bridges and hydrogen bonds, in accordance with the recently proposed "charge-zipper" motif.
Keyphrases
- molecular dynamics simulations
- molecular dynamics
- escherichia coli
- induced apoptosis
- molecular docking
- biofilm formation
- pseudomonas aeruginosa
- staphylococcus aureus
- cell cycle arrest
- solar cells
- candida albicans
- deep learning
- single molecule
- genome wide
- fluorescent probe
- fatty acid
- single cell
- endoplasmic reticulum stress
- gene expression
- machine learning
- cystic fibrosis
- stress induced
- oxidative stress
- heat stress
- wound healing
- transition metal