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The double membrane architecture of Gram-negative bacteria forms a barrier that is effectively impermeable to extracellular threats. Accordingly, researchers have shown increasing interest in developing antibiotics that target the accessible, surface-exposed proteins embedded in the outer membrane. TolC forms the outer membrane channel of an antibiotic efflux pump in Escherichia coli. Drawing from prior observations that colicin E1, a toxin produced by and lethal to E. coli, can bind to thedoi:10.1101/692251 fatcat:r4fupf3qczfwxjuojun4imy27e