ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2013
Structural mechanisms of heavy-metal extrusion by the Cus efflux system.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Contrasts and similarities in the transcriptomic response to antimicrobial coinage metals inMicrobiology spectrum · 2026Article
- The Resistance-Nodulation-Division efflux pump EefABC is highly conserved within lineages ofMicrobial genomics · 2026Article
- Mechanisms of Copper Selectivity and Release by the Metallochaperone CusF: Insights from CO-Binding, Rapid-Freeze-Quench EXAFS, and Unnatural Amino Acid Substitution.Inorganic chemistry · 2024Article
- The copper resistance mechanism in a newly isolated Pseudoxanthomonas spadix ZSY-33.Environmental microbiology reports · 2023Article
- Review
- Genomic and Transcriptomic Analysis Reveal Multiple Strategies for the Cadmium Tolerance inFoods (Basel, Switzerland) · 2022Article
- The Cell Membrane of a NovelCells · 2022Article
- Development of antibacterial compounds that constrain evolutionary pathways to resistance.eLife · 2021Article
- Targeting the Copper Transport System to Improve Treatment Efficacies of Platinum-Containing Drugs in Cancer Chemotherapy.Pharmaceuticals (Basel, Switzerland) · 2021Review
- TheThe Journal of biological chemistry · 2019Article
- Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.Communications biology · 2019Article
- Trapping intermediates in metal transfer reactions of the CusCBAF export pump ofCommunications biology · 2018Article
- Adaptor protein mediates dynamic pump assembly for bacterial metal efflux.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- EPR Spectroscopy Targets Structural Changes in the E. coli Membrane Fusion CusB upon Cu(I) Binding.Biophysical journal · 2017Article
- Novel Metal Cation Resistance Systems from Mutant Fitness Analysis of Denitrifying Pseudomonas stutzeri.Applied and environmental microbiology · 2016Article
- Heavy metal transport by the CusCFBA efflux system.Protein science : a publication of the Protein Society · 2015Review
- Unprecedented Silver Resistance in Clinically Isolated Enterobacteriaceae: Major Implications for Burn and Wound Management.Antimicrobial agents and chemotherapy · 2015Article
- The ins and outs of RND efflux pumps in Escherichia coli.Frontiers in microbiology · 2015Review
- Mechanism of coupling drug transport reactions located in two different membranes.Frontiers in microbiology · 2015Review
- The ins and outs of bacterial iron metabolism.Molecular microbiology · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Resistance-nodulation-cell division (RND) superfamily efflux systems are responsible for the active transport of toxic compounds from the Gram-negative bacterial cell. These pumps typically assemble as tripartite complexes, spanning the inner and outer membranes of the cell envelope. In Escherichia coli, the CusC(F)BA complex, which exports copper(I) and silver(I) and mediates resistance to these two metal ions, is the only known RND transporter with a specificity for heavy metals. We have determined the crystal structures of both the inner membrane pump CusA and membrane fusion protein CusB, as well as the adaptor-transporter CusBA complex formed by these two efflux proteins. In addition, the crystal structures of the outer membrane channel CusC and the periplasmic metallochaperone CusF have been resolved. Based on these structures, the entire assembled model of the tripartite efflux system has been developed, and this efflux complex should be in the form of CusC3-CusB6-CusA3. It has been shown that CusA utilizes methionine clusters to bind and export Cu(I) and Ag(I). This pump is likely to undergo a conformational change, and utilize a relay network of methionine clusters as well as conserved charged residues to extrude the metal ions from the bacterial cell.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.