ArticleThe Journal of membrane biology2003
Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases.
Article in The Journal of membrane biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.
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Who cites it
127 citing papers in PubMed.
- The transcriptional regulator CueR positively regulates the expression of theMicrobiology spectrum · 2026Article
- 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
- Phenotypic and genomic characterization of lead tolerance and Pb(II) removal by Klebsiella pneumoniae ST86 EP-L-21.Folia microbiologica · 2026Article
- Systematic mining and characterization of metal transporter families regulating zinc homeostasis provide insights into metal homeostasis inFrontiers in plant science · 2026Article
- Copper resistance in the cold: Genome analysis and characterisation of a PEnvironmental microbiology reports · 2024Article
- Mechanisms of microbial resistance against cadmium - a review.Journal of environmental health science & engineering · 2024Review
- A two-sequence motif-based method for the inventory of gene families in fragmented and poorly annotated genome sequences.BMC genomics · 2024Article
- Unraveling the Role of Metals and Organic Acids in Bacterial Antimicrobial Resistance in the Food Chain.Antibiotics (Basel, Switzerland) · 2023Review
- Zinc homeostasis in Pseudomonas.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- Direct Effects of Toxic Divalent Cations on Contractile Proteins with Implications for the Heart: Unraveling Mechanisms of Dysfunction.International journal of molecular sciences · 2023Review
- Copper Efflux System Required in Murine Lung Infection by Haemophilus influenzae Composed of a Canonical ATPase Gene and Tandem Chaperone Gene Copies.Infection and immunity · 2023Article
- Five copper homeostasis gene clusters encode the Cu-efflux resistome of the highly copper-tolerantPeerJ · 2023Article
- Characterization of three predicted zinc exporters inFrontiers in veterinary 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
- Mycobacterial resistance to zinc poisoning requires assembly of P-ATPase-containing membrane metal efflux platforms.Nature communications · 2022Article
- A Novel Zinc Exporter CtpG Enhances Resistance to Zinc Toxicity and Survival in Mycobacterium bovis.Microbiology spectrum · 2022Article
- Primary nutrient sensors in plants.iScience · 2022Review
- Structure and ion-release mechanism of PeLife · 2021Article
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
67 more citing papers are in PubMed but not listed here.
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1 author.
Funding
Abstract
P1B-type ATPases transport a variety of metals (Cd2+, Zn2+, Pb2+, Co2+, Cu2+, Ag+, Cu+) across biomembranes. Characteristic sequences CP[C/H/S] in transmembrane fragment H6 were observed in the putative transporting metal site of the founding members of this subfamily (initially named CPx-ATPases). In spite of their importance for metal homeostasis and biotolerance, their mechanisms of ion selectivity are not understood. Studies of better-characterized P(II)-type ATPases (Ca-ATPase and Na,K-ATPase) have identified three transmembrane segments that participate in ion binding and transport. Testing the hypothesis that metal specificity is determined by conserved amino acids located in the equivalent transmembrane segments of P1B-type ATPases (H6, H7, and H8), 234 P1B-ATPase protein sequences were analyzed. This showed that although H6 contains characteristic CPX or XPC sequences, conserved amino acids in H7 and H8 provide signature sequences that predict the metal selectivity in each of five P1B-ATPase subgroups identified. These invariant amino acids contain diverse side chains (thiol, hydroxyl, carbonyl, amide, imidazolium) that can participate in transient metal coordination during transport and consequently determine the particular metal selectivity of each enzyme. Each subgroup shares additional structural characteristics such as the presence (or absence) of particular amino-terminal metal-binding domains and the number of putative transmembrane segments. These differences suggest unique functional characteristics for each subgroup in addition to their particular metal specificity.
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