Bacterial Metal Resistance: Coping with Copper without Cooperativity?

mBio. 2021 Jun 29;12(3):e0065321. doi: 10.1128/mBio.00653-21. Epub 2021 Jun 15.

Abstract

In Escherichia coli and other Gram-negative bacteria, tripartite efflux pumps (TEPs) span the entire cell envelope and serve to remove noxious molecules from the cell. CusBCA is a TEP responsible for copper and silver detoxification in E. coli powered by the resistance-nodulation-cell division (RND) transporter, CusA. In a recent study, Moseng et al. (M. A. Moseng, M. Lyu, T. Pipatpolkai, P. Glaza, et al., mBio 12:e00452-21, 2021, https://dx.doi.org/10.1128/mBio.00452-21) obtained cryo-electron microscopy (cryo-EM) structures of CusA trimers in the presence of copper. The multiple conformations revealed suggest that the three monomers function independently within the CusA trimer, contrary to the cooperative mechanism proposed for the multidrug exporting RND transporter, AcrB. The work prompts consideration of the mechanism of this class of transporter and provides a basis to underpin further studies of TEPs important for bacterial survival.

Keywords: bacterial metal resistance; membrane proteins; tripartite efflux pumps.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Adaptation, Psychological
  • Copper / metabolism
  • Cryoelectron Microscopy
  • Escherichia coli Proteins* / metabolism
  • Escherichia coli* / genetics
  • Escherichia coli* / metabolism
  • Multidrug Resistance-Associated Proteins

Substances

  • AcrB protein, E coli
  • Escherichia coli Proteins
  • Multidrug Resistance-Associated Proteins
  • Copper