The Mechanism of Cu+ Transport ATPases

Padilla‐Benavides, Teresita; McCann, Courtney J.; Argüello, José M.

doi:10.1074/jbc.m112.420810

Cited by 72 publications

(55 citation statements)

References 42 publications

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“…6b) [66]. In some instances, these MBDs have been shown to be able to receive Cu + ions from Atx1-like metallochaperones, and Cu + binding by these domains alters ATPase activity as well as intracellular localization of the enzyme [54, 67, 68]. The function of these MBDs remains controversial [32, 68–72], but it would be logical for these domains to represent allosteric regulation in higher organisms, since metal homeostasis in eukaryotes is more complex than in prokaryotes, as has been previously suggested [32, 73].…”

Section: Resultsmentioning

confidence: 99%

Diversity of the metal-transporting P1B-type ATPases

2014

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The P1B-ATPases are integral membrane proteins that couple ATP hydrolysis to metal cation transport. Widely distributed across all domains of life, these enzymes have been previously shown to transport copper, zinc, cobalt, and other thiophilic heavy metals. Recent data suggest that these enzymes may also be involved in nickel and/or iron transport. Here we have exploited large amounts of genomic data to examine and classify the various P1B-ATPase subfamilies. Specifically, we have combined new methods of data partitioning and network visualization known as Transitivity Clustering and Protein Similarity Networks with existing biochemical data to examine properties such as length, speciation, and metal-binding motifs of the P1B-ATPase subfamily sequences. These data reveal interesting relationships among the enzyme sequences of previously established subfamilies, indicate the presence of two new subfamilies, and suggest the existence of new regulatory elements in certain subfamilies. Taken together, these findings underscore the importance of P1B-ATPases in homeostasis of nearly every biologically relevant transition metal and provide an updated framework for future studies.

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Section: Resultsmentioning

confidence: 99%

Diversity of the metal-transporting P1B-type ATPases

2014

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“…Other metal coordinating residues include His-Pro or Cys-Pro-Cys/His motif resides within the 6 th membrane-spanning helix as well as YN and MXXS in other transmembrane segments 17, 19 . The delivery of copper to these exporters is facilitated by copper chaperones, which are thought to interact electrostatically with the cytoplasmic amino terminal copper-binding domain of their cognate P 1B -type ATPases 20 . Although most copper chaperones are soluble proteins (e.g., the CopZ protein of Enterococcus hirae ), a recently discovered example of a membrane-bound variety is CupA, which has been found in lactobacilli and streptococci lacking a CopZ-like soluble metallochaperone 21 .…”

Section: Introductionmentioning

confidence: 99%

Copper tolerance and virulence in bacteria

2015

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Copper (Cu) is an essential trace element for all aerobic organisms. It functions as a cofactor in enzymes that catalyze a wide variety of redox reactions due to its ability to cycle between two oxidation states, Cu(I) and Cu(II). This same redox property of copper has the potential to cause toxicity if copper homeostasis is not maintained. Studies suggest that the toxic properties of copper are harnessed by the innate immune system of the host to kill bacteria. To counter such defenses, bacteria rely on copper tolerance genes for virulence within the host. These discoveries suggest bacterial copper intoxication is a component of host nutritional immunity, thus expanding our knowledge of the roles of copper in biology. This review summarizes our current understanding of copper tolerance in bacteria, and the extent to which these pathways contribute to bacterial virulence within the host.

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“…Then, it was proposed that the platform might serve as a landing pad for the chaperone-ATPase interaction, as the invariant residues might be involved in ligand exchange and Cu + transfer to the TM-MBSs 52 . Subsequent studies yielded experimental evidence consistent with this hypothesis 64 . On the other hand, Cu + extrusion through a specific permeation path with participation of invariant Met and Glu amino acids has been proposed 53 .…”

Section: The Molecular Structure Responsible For Copper Transmembranementioning

confidence: 81%

“…Upon specific docking, Cu + is transferred via ligand exchange. This Cu + exchange between CopZ and N-MBDs is independent of the delivery of Cu + to the ATPase permeation path for transmembrane transport 64, 86 (see below).…”

Section: Chaperone Mediated Ion Uptake and Release Of Cu+-atpasesmentioning

confidence: 99%

Bacterial Cu⁺-ATPases: models for molecular structure–function studies

2016

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The early discovery of the human Cu+-ATPases and their link to Menkes and Wilson's diseases brought attention to the unique role of these transporters in copper homeostasis. The characterization of bacterial Cu+-ATPases has significantly furthered our understanding on the structure, selectivity and transport mechanism of these enzymes, as well as their interplay with other elements of Cu+ distribution networks. This review focuses on the structural-functional insights that have emerged from studies of bacterial Cu+-ATPase at the molecular level and how these observations have contributed to draw up a comprehensive picture of cellular copper homeostasis.

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The Mechanism of Cu+ Transport ATPases

Abstract: Background: Cytoplasmic chaperones deliver Cu ϩ to P 1B -ATPases for outward transport.

Cited by 72 publications

References 42 publications

Diversity of the metal-transporting P1B-type ATPases

Diversity of the metal-transporting P1B-type ATPases

Copper tolerance and virulence in bacteria

Bacterial Cu⁺-ATPases: models for molecular structure–function studies

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The Mechanism of Cu+ Transport ATPases

Abstract: Background: Cytoplasmic chaperones deliver Cu ϩ to P 1B -ATPases for outward transport.

Cited by 72 publications

References 42 publications

Diversity of the metal-transporting P1B-type ATPases

Diversity of the metal-transporting P1B-type ATPases

Copper tolerance and virulence in bacteria

Bacterial Cu+-ATPases: models for molecular structure–function studies

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Product

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Bacterial Cu⁺-ATPases: models for molecular structure–function studies