ArticleEMBO reports2015
A sulfur-based transport pathway in Cu+-ATPases.
Article in EMBO reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed.
- Preparation of Plasma Membrane Vesicles, Lysosomes, Proteoliposomes and Alternative Sample Types for SSM-Based Electrophysiology.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Transition metal transporting P-type ATPases: terminal metal-binding domains serve as sensors for autoinhibitory tails.The FEBS journal · 2025Article
- Non-hyperbolic enzyme kinetics: the case of P-type ATPases.Biophysical reviews · 2025Review
- Mammalian copper homeostasis: physiological roles and molecular mechanisms.Physiological reviews · 2025Review
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases.Nature communications · 2024Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Copper binding leads to increased dynamics in the regulatory N-terminal domain of full-length human copper transporter ATP7B.PLoS computational biology · 2022Article
- Structural basis of ion uptake in copper-transporting PNature communications · 2022Article
- Structure and ion-release mechanism of PeLife · 2021Article
- Targeting the Copper Transport System to Improve Treatment Efficacies of Platinum-Containing Drugs in Cancer Chemotherapy.Pharmaceuticals (Basel, Switzerland) · 2021Review
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Transmembrane Cu(I) P-type ATPase pumps are electrogenic uniporters.Dalton transactions (Cambridge, England : 2003) · 2020Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Protein Adsorption on Solid Supported Membranes: Monitoring the Transport Activity of P-Type ATPases.Molecules (Basel, Switzerland) · 2020Review
- Label-Free Bioelectrochemical Methods for Evaluation of Anticancer Drug Effects at a Molecular Level.Sensors (Basel, Switzerland) · 2020Review
- Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Catalytic M Center of Copper Monooxygenases Probed by Rational Design. Effects of Selenomethionine and Histidine Substitution on Structure and Reactivity.Biochemistry · 2019Article
- Review
- Rational Design of a Histidine-Methionine Site Modeling the M-Center of Copper Monooxygenases in a Small Metallochaperone Scaffold.Biochemistry · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Cells regulate copper levels tightly to balance the biogenesis and integrity of copper centers in vital enzymes against toxic levels of copper. PIB -type Cu(+)-ATPases play a central role in copper homeostasis by catalyzing the selective translocation of Cu(+) across cellular membranes. Crystal structures of a copper-free Cu(+)-ATPase are available, but the mechanism of Cu(+) recognition, binding, and translocation remains elusive. Through X-ray absorption spectroscopy, ATPase activity assays, and charge transfer measurements on solid-supported membranes using wild-type and mutant forms of the Legionella pneumophila Cu(+)-ATPase (LpCopA), we identify a sulfur-lined metal transport pathway. Structural analysis indicates that Cu(+) is bound at a high-affinity transmembrane-binding site in a trigonal-planar coordination with the Cys residues of the conserved CPC motif of transmembrane segment 4 (C382 and C384) and the conserved Met residue of transmembrane segment 6 (M717 of the MXXXS motif). These residues are also essential for transport. Additionally, the studies indicate essential roles of other conserved intramembranous polar residues in facilitating copper binding to the high-affinity site and subsequent release through the exit pathway.
Indexed as
Identifiers
What OpenQuestion holds
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.