ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012
Structure and mechanism of the tripartite CusCBA heavy-metal efflux complex.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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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
42 citing papers in PubMed, 80 citations in OpenAlex.
- Comprehensive genomic analysis of avian Escherichia coli from Noakhali uncovers multidrug resistance, metal resistance, and zoonotic signatures.Scientific reports · 2026Article
- CuiT is a Cu importer required for metal homeostasis inBiochemistry and biophysics reports · 2026Article
- Microbial functional traits in the hyperaccumulating Noccaea praecox rhizobiome are metal-dependent and host-driven.Environmental microbiome · 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
- Drug resistance and physiological roles of RND multidrug efflux pumps inMicrobiology (Reading, England) · 2023Article
- The culmination of multidrug-resistant efflux pumps vs. meager antibiotic arsenal era: Urgent need for an improved new generation of EPIs.Frontiers in microbiology · 2023Review
- What Approaches to Thwart Bacterial Efflux Pumps-Mediated Resistance?Antibiotics (Basel, Switzerland) · 2022Review
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Bacterial Multidrug Efflux Pumps at the Frontline of Antimicrobial Resistance: An Overview.Antibiotics (Basel, Switzerland) · 2022Review
- NMR reveals the interplay between SilE and SilB model peptides in the context of silver resistance.Chemical communications (Cambridge, England) · 2021Article
- Article
- Molecular Insights into the Copper-Sensitive Operon Repressor in Acidithiobacillus caldus.Applied and environmental microbiology · 2021Article
- Structural and Functional Diversity of Resistance-Nodulation-Cell Division Transporters.Chemical reviews · 2021Review
- Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.Chemical reviews · 2021Review
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- RNase I ModulatesACS chemical biology · 2020Article
- Comparative Insights Into the Complete Genome Sequence of Highly Metal ResistantFrontiers in microbiology · 2020Article
- Comparative Genomics ofFrontiers in microbiology · 2019Article
- Crystal structures of AztD provide mechanistic insights into direct zinc transfer between proteins.Communications biology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Gram-negative bacteria frequently expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membranes. The three parts are the inner membrane, substrate-binding transporter (or pump); a periplasmic membrane fusion protein (MFP, or adaptor); and an outer membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. One such efflux system CusCBA is responsible for extruding biocidal Cu(I) and Ag(I) ions. We previously described the crystal structures of both the inner membrane transporter CusA and the MFP CusB of Escherichia coli. We also determined the co-crystal structure of the CusBA adaptor-transporter efflux complex, showing that the transporter CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. Here, we summarize the structural information of these efflux proteins, and present the accumulated evidence that this efflux system uses methionine residues to bind and export Cu(I) and Ag(I). Genetic and structural analyses suggest that the CusA pump is capable of picking up the metal ions from both the periplasm and the cytoplasm. We propose a stepwise shuttle mechanism for this pump to export metal ions from the 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.