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TitleColicin E1 opens its hinge to plug TolC.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateFeb 24, 2022
AuthorsS Jimmy Budiardjo / Jacqueline J Stevens / Anna L Calkins / Ayotunde P Ikujuni / Virangika K Wimalasena / Emre Firlar / David A Case / Julie S Biteen / Jason T Kaelber / Joanna S G Slusky /
PubMed AbstractThe 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 ...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, 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 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.
External linksElife / PubMed:35199644 / PubMed Central
MethodsEM (single particle)
Resolution2.84 - 3.09 Å
Structure data

21959

6wxh

EMDB-21959, PDB-6wxh:
Colicin E1 fragment in nanodisc-embedded TolC
Method: EM (single particle) / Resolution: 3.09 Å

21960

6wxi

EMDB-21960, PDB-6wxi:
Colicin E1 fragment in nanodisc-embedded TolC
Method: EM (single particle) / Resolution: 2.84 Å

Source
  • Escherichia coli K-12 (bacteria)
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
KeywordsANTIMICROBIAL PROTEIN / antibiotic efflux / bacteriocin / TRANSPORT PROTEIN

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