ArticleCurrent topics in membranes2012
Toward a molecular understanding of metal transport by P(1B)-type ATPases.
Article in Current topics in membranes, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 69 citations in OpenAlex.
- The genes zntA and zntR encoding a P-type ATPase and its activator confer zinc and cadmium resistance in Chromobacterium violaceum.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026Article
- Effluxosomes and the evolution of metal resistance inInfection and immunity · 2026Review
- Article
- Generative Landscapes and Dynamics to Design Functional Multidomain Artificial Transmembrane Transporters.ACS central science · 2025Article
- Review
- Non-hyperbolic enzyme kinetics: the case of P-type ATPases.Biophysical reviews · 2025Review
- In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024Review
- In a state of flux: new insight into the transport processes that maintain bacterial metal homeostasis.Journal of bacteriology · 2024Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Article
- Is Genetic Engineering a Route to Enhance Microalgae-Mediated Bioremediation of Heavy Metal-Containing Effluents?Molecules (Basel, Switzerland) · 2022Review
- Structure and ion-release mechanism of PeLife · 2021Article
- Membrane Transporters Involved in the Antimicrobial Activities of Pyrithione inMolecules (Basel, Switzerland) · 2021Article
- Article
- 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
- Characterization of the copper resistance mechanism and bioremediation potential of an Acinetobacter calcoaceticus strain isolated from copper mine sludge.Environmental science and pollution research international · 2020Article
- di-Cysteine Residues of theFrontiers in plant science · 2020Article
- Pull-Down of Metalloproteins in Their Native States by Using Desthiobiotin-Based Probes.Chembiochem : a European journal of chemical biology · 2019Article
- The Cu chaperone CopZ is required for Cu homeostasis in Rhodobacter capsulatus and influences cytochrome cbbMolecular microbiology · 2019Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
The P(1B) family of P-type ATPases couples the transport of cytoplasmic transition metals across biological membranes to the hydrolysis of ATP. These ubiquitous transporters function in maintaining cytoplasmic metal quotas and in the assembly of metalloproteins, and have been classified into subfamilies (P(1B-1)-P(1B-5)) on the basis of their transported substrates (Cu(+), Zn(2+), Cu(2+), and Co(2+)) and signature sequences in their transmembrane segments. In addition, each subgroup presents a characteristic membrane topology and specific regulatory cytoplasmic metal-binding domains. In recent years, significant major aspects of their transport mechanism have been described, including the stoichiometry of transport and the delivery of substrates to transport sites by metallochaperones. Toward understanding their structure, the metal coordination by transport sites has been characterized for Cu(+) and Zn(2+)-ATPases. In addition, atomic resolution structures have been determined, providing key insight into the elements that enable transition metal transport. Because the Cu(+)-transporting ATPases are found in humans and are linked to disease, this subfamily has been the focus of intense study. As a result, significant progress has been made toward understanding Cu(+)-ATPase function on the molecular level, using both the human proteins and the bacterial homologs, most notably the CopA proteins from Archaeoglobus fulgidus, Bacillus subtilis, and Thermotoga maritima. This chapter thus focuses on the mechanistic and structural information obtained by studying these latter Cu(+)-ATPases, with some consideration of how these aspects might differ for the other subfamilies of P(1B)-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.