ReviewBiochemistry2011
Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence.
Review in Biochemistry, 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, 113 citations in OpenAlex.
- Small RNA Transcriptome of the Oral Microbiome during Periodontitis Progression.Applied and environmental microbiology · 2015Trial
- Article
- 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
- A broad-spectrum inhibitor of copper-exporting PProceedings of the National Academy of Sciences of the United States of America · 2026Article
- A First-In-Class Broad Spectrum Inhibitor of Copper Exporting PbioRxiv : the preprint server for biology · 2026Article
- A review on simultaneous use of microbes and biochar for removal of toxic heavy metals: Recent updates and future outlooks.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Review
- Draft genome sequence of '3 Biotech · 2024Article
- Fluorescence-Based Proteoliposome Methods to Monitor Redox-Active Transition Metal Transmembrane Translocation by Metal Transporters.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Plastic recognition and electrogenic uniport translocation of 1Chemical science · 2023Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Computational identification of putative copper-binding proteins in pomegranate bacterial blight pathogen Xanthomonas citri pv. punicae.Archives of microbiology · 2022Article
- Environmental Conditions Modulate the Transcriptomic Response of BothMicroorganisms · 2021Article
- Zinc: Multidimensional Effects on Living Organisms.Biomedicines · 2021Review
- 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
- Article
- Cadmium Uptake by Wheat (Plants (Basel, Switzerland) · 2020Review
- Shotgun proteomic analysis of nanoparticle-synthesizingMicrobiology (Reading, England) · 2019Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
P(1B)-type ATPases are polytopic membrane proteins that couple the hydrolysis of ATP to the efflux of cytoplasmic transition metals. This paper reviews recent progress in our understanding of the structure and function of these proteins in bacteria. These are members of the P-type superfamily of transport ATPases. Cu(+)-ATPases are the most frequently observed and best-characterized members of this group of transporters. However, bacterial genomes show diverse arrays of P(1B)-type ATPases with a range of substrates (Cu(+), Zn(2+), Co(2+)). Furthermore, because of the structural similarities among transitions metals, these proteins can also transport nonphysiological substrates (Cd(2+), Pb(2+), Au(+), Ag(+)). P(1B)-type ATPases have six or eight transmembrane segments (TM) with metal coordinating amino acids in three core TMs flanking the cytoplasmic domain responsible for ATP binding and hydrolysis. In addition, regulatory cytoplasmic metal binding domains are present in most P(1B)-type ATPases. Central to the transport mechanism is the binding of the uncomplexed metal to these proteins when cytoplasmic substrates are bound to chaperone and chelating molecules. Metal binding to regulatory sites is through a reversible metal exchange among chaperones and cytoplasmic metal binding domains. In contrast, the chaperone-mediated metal delivery to transport sites appears as a largely irreversible event. P(1B)-ATPases have two overarching physiological functions: to maintain cytoplasmic metal levels and to provide metals for the periplasmic assembly of metalloproteins. Recent studies have shown that both roles are critical for bacterial virulence, since P(1B)-ATPases appear key to overcome high phagosomal metal levels and are required for the assembly of periplasmic and secreted metalloproteins that are essential for survival in extreme oxidant 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.