ArticleNature chemical biology2015
A new metal binding domain involved in cadmium, cobalt and zinc transport.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- The hazards of metal exposure mediated by crops to human health from perspective of environmental health and control strategies.iScience · 2026Review
- Transition metal transporting P-type ATPases: terminal metal-binding domains serve as sensors for autoinhibitory tails.The FEBS journal · 2025Article
- Genome-wide identification of heavy-metal ATPases genes in Areca catechu: investigating their functionality under heavy metal exposure.BMC plant biology · 2024Article
- Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Interplay between Two-Component Regulatory Systems Is Involved in Control of Cupriavidus metallidurans Metal Resistance Genes.Journal of bacteriology · 2023Article
- Metalloprotein-Specific or Critical Amino Acid Residues: Perspectives on Plant-Precise Detoxification and Recognition Mechanisms under Cadmium Stress.International journal of molecular sciences · 2022Review
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
- Stabilization of supramolecular membrane protein-lipid bilayer assemblies through immobilization in a crystalline exoskeleton.Nature communications · 2021Article
- The CopA2-Type PFrontiers in microbiology · 2021Article
- Prediction of Metal Ion Binding Sites of Transmembrane Proteins.Computational and mathematical methods in medicine · 2021Article
- Genomic Insights Into Cadmium Resistance of a Newly Isolated, Plasmid-FreeFrontiers in microbiology · 2021Article
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Cobalt Resistance via Detoxification and Mineralization in the Iron-Reducing BacteriumFrontiers in microbiology · 2020Article
- Unique roles of iron and zinc binding to the yeast Fe-S cluster scaffold assembly protein "Isu1".Metallomics : integrated biometal science · 2019Article
- Characterization of a promiscuous cadmium and arsenic resistance mechanism in Thermus thermophilus HB27 and potential application of a novel bioreporter system.Microbial cell factories · 2018Article
- CuProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Metal Selectivity of a Cd-, Co-, and Zn-Transporting PBiochemistry · 2017Article
- Fine-tuning of Substrate Affinity Leads to Alternative Roles of Mycobacterium tuberculosis Fe2+-ATPases.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The P1B-ATPases, which couple cation transport across membranes to ATP hydrolysis, are central to metal homeostasis in all organisms. An important feature of P1B-ATPases is the presence of soluble metal binding domains (MBDs) that regulate transport activity. Only one type of MBD has been characterized extensively, but bioinformatics analyses indicate that a diversity of MBDs may exist in nature. Here we report the biochemical, structural and functional characterization of a new MBD from the Cupriavidus metallidurans P1B-4-ATPase CzcP (CzcP MBD). The CzcP MBD binds two Cd(2+), Co(2+) or Zn(2+) ions in distinct and unique sites and adopts an unexpected fold consisting of two fused ferredoxin-like domains. Both in vitro and in vivo activity assays using full-length CzcP, truncated CzcP and several variants indicate a regulatory role for the MBD and distinct functions for the two metal binding sites. Taken together, these findings elucidate a previously unknown MBD and suggest new regulatory mechanisms for metal transport by P1B-ATPases.
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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.