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Identification of Ion-Selectivity Determinants in Heavy-Metal Transport P1B-type ATPases
  • J. Argüello
  • Biology
    The Journal of Membrane Biology
  • 15 September 2003
TLDR
Testing the hypothesis that metal specificity is determined by conserved amino acids located in the equivalent transmembrane segments of P1B-type ATPases showed that although H6 contains characteristic CPX or XPC sequences, conserving amino acids in H7 and H8 provide signature sequences that predict the metal selectivity in each of five P 1B-ATPase subgroups identified.
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The structure and function of heavy metal transport P1B-ATPases
TLDR
The current knowledge of structure-function relationships among the different P1B- ATPases allows for a description of selectivity, regulation and transport mechanisms and provides a framework to understand mutations in human Cu+-ATPases (ATP7A and ATP7B) that lead to Menkes and Wilson diseases.
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Mechanism of Cu+-transporting ATPases: Soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites
TLDR
Testing both models, the delivery of Cu+ by Archaeoglobus fulgidus Cu+ chaperone CopZ to the corresponding Cu+-ATPase, CopA, was studied, and under nonturnover conditions, CopZ transferred Cu+ to the TM-MBS of a CopA lacking MBDs.
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Arabidopsis HMA2, a Divalent Heavy Metal-Transporting PIB-Type ATPase, Is Involved in Cytoplasmic Zn2+ Homeostasis1
TLDR
Results suggest that HMA2 is responsible for Zn2+ efflux from the cells and therefore is required for maintaining low cytoplasmic Zn 2+ levels and normal Zn1+ homeostasis.
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Characterization of a Thermophilic P-type Ag+/Cu+-ATPase from the ExtremophileArchaeoglobus fulgidus*
TLDR
CopA is described, the first Ag+/Cu+-ATPase expressed and purified in a functional form, and provides a model for structure-functional studies of thermophilic ion transporters.
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Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase.
TLDR
On the basis of sequence and structural comparisons, specific residues that probably interact with the CopA ATPBD have been identified and the presence of an additional loop that may be associated with regulatory functions in eukaryotic Cu(+)-ATPases is revealed.
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Structure of the ATP Binding Domain from the Archaeoglobus fulgidus Cu+-ATPase*
TLDR
The structure of the CopA ATP binding domain (ATPBD) provides a basis for understanding the likely structural and functional effects of various mutations that lead to Wilson and Menkes diseases.
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Distinct functional roles of homologous Cu+ efflux ATPases in Pseudomonas aeruginosa
TLDR
Pseudomonas aeruginosa has two structurally similar Cu+‐ATPases, CopA1 and CopA2, but it is hypothesize that their distinct cellular functions could be based on the intrinsic differences in transport kinetic or the likely requirement of periplasmic partner Cu‐chaperone proteins specific for each Cu-ATPase.
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Mechanisms of copper homeostasis in bacteria
TLDR
Recent studies based on biochemical, bioinformatics, and metalloproteomics approaches, reveal a highly regulated system of transcriptional regulators, soluble chaperones, membrane transporters, and target cuproproteins distributed in the various bacterial compartments.
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Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA.
TLDR
The data suggest a regulatory mechanism in which the Cu-dependent N-MBD/ATP binding domain interaction would accelerate cation release, the enzyme rate-limiting step, and consequently Cu(+) transport.
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