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- W4213425437 abstract "The double membrane architecture of Gram-negative bacteria forms a barrier that is impermeable to most extracellular threats. Bacteriocin proteins evolved to exploit the accessible, surface-exposed proteins embedded in the outer membrane to deliver cytotoxic cargo. Colicin E1 is a bacteriocin produced by, and lethal to, Escherichia coli that hijacks the outer membrane proteins (OMPs) TolC and BtuB to enter the cell. Here, we capture the colicin E1 translocation domain inside its membrane receptor, TolC, by high-resolution cryo-electron microscopy to obtain the first reported structure of a bacteriocin bound to TolC. Colicin E1 binds stably to TolC as an open hinge through the TolC pore—an architectural rearrangement from colicin E1’s unbound conformation. This binding is stable in live E. coli cells as indicated by single-molecule fluorescence microscopy. Finally, colicin E1 fragments binding to TolC plug the channel, inhibiting its native efflux function as an antibiotic efflux pump, and heightening susceptibility to three antibiotic classes. In addition to demonstrating that these protein fragments are useful starting points for developing novel antibiotic potentiators, this method could be expanded to other colicins to inhibit other OMP functions." @default.
- W4213425437 created "2022-02-25" @default.
- W4213425437 creator A5002522596 @default.
- W4213425437 creator A5004199608 @default.
- W4213425437 creator A5014694160 @default.
- W4213425437 creator A5023598281 @default.
- W4213425437 creator A5031330750 @default.
- W4213425437 creator A5037499835 @default.
- W4213425437 creator A5053537139 @default.
- W4213425437 creator A5053735436 @default.
- W4213425437 creator A5072366014 @default.
- W4213425437 creator A5084223077 @default.
- W4213425437 date "2022-02-24" @default.
- W4213425437 modified "2023-10-18" @default.
- W4213425437 title "Colicin E1 opens its hinge to plug TolC" @default.
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