ArticleBiometals : an international journal on the role of metal ions in biology, biochemistry, and medicine2011
The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function.
Article in Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 119 citations in OpenAlex.
- Article
- The gonococcal vaccine candidate antigen NGO1701 is a N. gonorrhoeae periplasmic copper storage protein.PLoS pathogens · 2025Article
- Tetranucleotide frequencies differentiate genomic boundaries and metabolic strategies across environmental microbiomes.mSystems · 2025Article
- Review
- The Plasma Membrane P-Type ATPase CtpA Is Required forBiomedicines · 2025Article
- Aqueous copper geochemistry shapes the sediment microbial resistome in a recovering stream.Environmental microbiology reports · 2024Article
- Discriminating Susceptibility of Xanthine Oxidoreductase Family to Metals.Microbiology spectrum · 2023Article
- Full Copper Resistance in Cupriavidus metallidurans Requires the Interplay of Many Resistance Systems.Applied and environmental microbiology · 2023Article
- Functional Characterization of the CoApplied and environmental microbiology · 2023Article
- Adaptive Mechanisms ofToxics · 2023Article
- Five copper homeostasis gene clusters encode the Cu-efflux resistome of the highly copper-tolerantPeerJ · 2023Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Contribution of a ZIP-family protein to manganese uptake and infective endocarditis virulence in Streptococcus sanguinis.Molecular microbiology · 2022Article
- Transcriptomics and Functional Analysis of Copper Stress Response in the Sulfate-Reducing BacteriumInternational journal of molecular sciences · 2022Article
- Copper Homeostatic Mechanisms and Their Role in the Virulence of Escherichia coli and Salmonella enterica.EcoSal Plus · 2021Review
- Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021Review
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- CtpB is a plasma membrane copper (I) transporting P-type ATPase of Mycobacterium tuberculosis.Biological research · 2020Article
- Comparative Insights Into the Complete Genome Sequence of Highly Metal ResistantFrontiers in microbiology · 2020Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Cu(+)-ATPases play a key role in bacterial Cu(+) homeostasis by participating in Cu(+) detoxification and cuproprotein assembly. Characterization of Archaeoglobus fulgidus CopA, a model protein within the subfamily of P(1B-1) type ATPases, has provided structural and mechanistic details on this group of transporters. Atomic resolution structures of cytoplasmic regulatory metal binding domains (MBDs) and catalytic actuator, phosphorylation, and nucleotide binding domains are available. These, in combination with whole protein structures resulting from cryo-electron microscopy analyses, have enabled the initial modeling of these transporters. Invariant residues in helixes 6, 7 and 8 form two transmembrane metal binding sites (TM-MBSs). These bind Cu(+) with high affinity in a trigonal planar geometry. The cytoplasmic Cu(+) chaperone CopZ transfers the metal directly to the TM-MBSs; however, loading both of the TM-MBSs requires binding of nucleotides to the enzyme. In agreement with the classical transport mechanism of P-type ATPases, occupancy of both transmembrane sites by cytoplasmic Cu(+) is a requirement for enzyme phosphorylation and subsequent transport into the periplasmic or extracellular milieus. Recent transport studies have shown that all Cu(+)-ATPases drive cytoplasmic Cu(+) efflux, albeit with quite different transport rates in tune with their various physiological roles. Archetypical Cu(+)-efflux pumps responsible for Cu(+) tolerance, like the Escherichia coli CopA, have turnover rates ten times higher than those involved in cuproprotein assembly (or alternative functions). This explains the incapability of the latter group to significantly contribute to the metal efflux required for survival in high copper environments.
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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.