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Colicin E1 opens its hinge to plug TolC.

S Jimmy Budiardjo1, Jacqueline J Stevens2, Anna L Calkins3

  • 1Center for Computational Biology, The University of Kansas, Lawrence, United States.

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|February 24, 2022
PubMed
Summary
This summary is machine-generated.

Bacteriocin proteins like colicin E1 can block essential bacterial outer membrane channels. This structural study reveals how colicin E1 inhibits TolC, offering new strategies for antibiotic development.

Keywords:
E. coliTolCantibiotic effluxantibiotic resistancecolicincolicin E1infectious diseasemicrobiologymolecular biophysicsstructural biology

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Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Gram-negative bacteria possess a protective outer membrane.
  • Bacteriocins, such as colicin E1, target outer membrane proteins (OMPs) for cell entry.
  • TolC is a crucial OMP involved in bacterial efflux and colicin entry.

Purpose of the Study:

  • To determine the structure of colicin E1 bound to its outer membrane receptor, TolC.
  • To investigate the mechanism of colicin E1 translocation and its effect on TolC function.
  • To explore the potential of colicin E1 fragments as antibiotic potentiators.

Main Methods:

  • High-resolution cryo-electron microscopy (cryo-EM) to visualize colicin E1-TolC complex.
  • Single-molecule fluorescence microscopy to assess binding stability in live bacteria.
  • Biochemical assays to evaluate the impact on TolC's efflux function.

Main Results:

  • The first high-resolution structure of a bacteriocin (colicin E1) bound to TolC was obtained.
  • Colicin E1 adopts an open-hinge conformation upon stable binding within the TolC pore.
  • Colicin E1 fragments were shown to inhibit TolC's antibiotic efflux activity, increasing bacterial susceptibility to antibiotics.

Conclusions:

  • Colicin E1 binding to TolC represents a significant conformational change, blocking its function.
  • Inhibiting TolC via colicin E1 fragments enhances antibiotic efficacy, suggesting potential as potentiators.
  • This structural and functional insight can guide the development of new strategies against Gram-negative bacteria and OMP-targeted therapeutics.