On the ion coupling mechanism of the MATE transporter ClbM

Alexander Krah (Lead / Corresponding author), Roland G. Huber, Ulrich Zachariae, Peter J. Bond

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)
99 Downloads (Pure)


Bacteria use a number of mechanisms to defend themselves from antimicrobial drugs. One important defense strategy is the ability to export drugs by multidrug transporters. One class of multidrug transporter, the so-called multidrug and toxic compound extrusion (MATE) transporters, extrude a variety of antibiotic compounds from the bacterial cytoplasm. These MATE transporters are driven by a Na+, H+, or combined Na+/H+ gradient, and act as antiporters to drive a conformational change in the transporter from the outward to the inward-facing conformation. In the inward-facing conformation, a chemical compound (drug) binds to the protein, resulting in a switch to the opposite conformation, thereby extruding the drug. Using molecular dynamics simulations, we now report the structural basis for Na+ and H+ binding in the dual ion coupled MATE transporter ClbM from Escherichia coli, which is connected to colibactin-induced genotoxicity, yielding novel insights into the ion/drug translocation mechanism of this bacterial transporter.

Original languageEnglish
Article number183137
Pages (from-to)1-9
Number of pages9
JournalBBA - Biomembranes
Issue number2
Early online date28 Nov 2019
Publication statusPublished - 1 Feb 2020


  • MATE transporter
  • MD simulations
  • Ion-translocation mechanism
  • Drug release mechanism

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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