Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 123, Issue 8, Pages 1770-1779Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.8b12087
Keywords
-
Categories
Funding
- German Research Foundation (DFG) [GRK 2039, UL 172/7-1, KU 3677/2]
- state of Baden-Wurttemberg through bwHPC
- DFG [INST 40/467-1 FUGG]
Ask authors/readers for more resources
TisB is a short amphiphilic alpha-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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available