ArticleProceedings of the National Academy of Sciences of the United States of America2014
Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
48 citing papers in PubMed, 102 citations in OpenAlex.
- Bioinformatic Resistome Profiling of Metal Tolerance Mechanisms in Endodontic Infections: Implications for Antimicrobial Nanoparticle-Based Biomaterials.Journal of functional biomaterials · 2026Article
- The exploitation of nutrient metals by bacteria for survival and infection in the gut.PLoS pathogens · 2025Review
- Comprehensive analysis of orthologous genes reveals functional dynamics and energy metabolism in the rhizospheric microbiome of Moringa oleifera.Functional & integrative genomics · 2025Article
- 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
- It Takes Two to Make a Thing Go Right: Epistasis, Two-Component Response Systems, and Bacterial Adaptation.Microorganisms · 2024Article
- Application of biofilm dispersion-based nanoparticles in cutting off reinfection.Applied microbiology and biotechnology · 2024Review
- Early transcriptional changes of heavy metal resistance and multiple efflux genes in Xanthomonas campestris pv. campestris under copper and heavy metal ion stress.BMC microbiology · 2024Article
- Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.Dalton transactions (Cambridge, England : 2003) · 2024Article
- The battle for silver binding: How the interplay between the SilE, SilF, and SilB proteins contributes to the silver efflux pump mechanism.The Journal of biological chemistry · 2023Article
- Spectroscopic and QM/MM studies of the Cu(I) binding site of the plant ethylene receptor ETR1.Biophysical journal · 2022Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Copper monooxygenase reactivity: Do consensus mechanisms accurately reflect experimental observations?Journal of inorganic biochemistry · 2022Article
- A role for the periplasmic adaptor protein AcrA in vetting substrate access to the RND efflux transporter AcrB.Scientific reports · 2022Article
- The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery.The Journal of biological chemistry · 2022Article
- Copper Homeostatic Mechanisms and Their Role in the Virulence of Escherichia coli and Salmonella enterica.EcoSal Plus · 2021Review
- NMR reveals the interplay between SilE and SilB model peptides in the context of silver resistance.Chemical communications (Cambridge, England) · 2021Article
- Article
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Recent advances in exploring the heavy metal(loid) resistant microbiome.Computational and structural biotechnology journal · 2021Review
- The bacterial copper resistance protein CopG contains a cysteine-bridged tetranuclear copper cluster.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Copper is an essential nutrient for all aerobic organisms but is toxic in excess. At the host-pathogen interface, macrophages respond to bacterial infection by copper-dependent killing mechanisms, whereas the invading bacteria are thought to counter with an up-regulation of copper transporters and efflux pumps. The tripartite efflux pump CusCBA and its metallochaperone CusF are vital to the detoxification of copper and silver ions in the periplasm of Escherichia coli. However, the mechanism of efflux by this complex, which requires the activation of the inner membrane pump CusA, is poorly understood. Here, we use selenomethionine (SeM) active site labels in a series of biological X-ray absorption studies at the selenium, copper, and silver edges to establish a "switch" role for the membrane fusion protein CusB. We determine that metal-bound CusB is required for activation of cuprous ion transfer from CusF directly to a site in the CusA antiporter, showing for the first time (to our knowledge) the in vitro activation of the Cus efflux pump. This metal-binding site of CusA is unlike that observed in the crystal structures of the CusA protein and is composed of one oxygen and two sulfur ligands. Our results suggest that metal transfer occurs between CusF and apo-CusB, and that, when metal-loaded, CusB plays a role in the regulation of metal ion transfer from CusF to CusA in the periplasm.
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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.