Journal
MBIO
Volume 12, Issue 3, Pages -Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/mBio.00653-21
Keywords
tripartite efflux pumps; bacterial metal resistance; membrane proteins
Categories
Funding
- Medical Research Council
- Wellcome Trust
- MRC [MR/N000994/1] Funding Source: UKRI
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The study shows that the three monomers within the CusA trimer can function independently in the presence of copper, contrary to the cooperative mechanism proposed for the multidrug exporting transporter. This provides a basis for further research on TEPs important for bacterial survival.
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.
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