On Allosteric Modulation of P-Type Cu+-ATPases

Mattle, D.; Sitsel, Oleg; Autzen, Henriette Elisabeth; Meloni, Gabriele; Gourdon, Pontus; Nissen, Poul

doi:10.1016/j.jmb.2013.03.008

Cited by 30 publications

(50 citation statements)

References 74 publications

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“…The kink exposes three invariant residues (one Met and two Glu) that enable ligand exchange between the chaperone and the transporter (10). After ligand exchange, the Cu + ions occupy the intramembrane metal-binding sites (11), and following the classic Albers-Post model, Cu + export requires the metal-dependent catalytic phosphorylation of an invariant Asp (DKTGT) (5,12,13).…”

Section: Atx1mentioning

confidence: 99%

“…Because this domain is not essential in vitro for activity (8,10), one plausible role for the HMBD is in autoregulation of the ATPase; Cu + delivery to this domain may be required before the chaperone can dock to the platform and deliver Cu + to the intramembrane metal-binding sites (13). Interestingly, the HMBDs of the Cu + -ATPases and the Atx1-like chaperones are structurally similar with a ferredoxin-like fold and bind Cu + through a conserved MxCxxC motif.…”

Section: Atx1mentioning

confidence: 99%

See 1 more Smart Citation

Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis

Blaby‐Haas¹,

Padilla‐Benavides

Stübe³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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+) from its point of entry at the plasma membrane to its destination. In plants, one destination is the chloroplast, which houses plastocyanin, a Cu-dependent electron transfer protein involved in photosynthesis. We present a previously unidentified Cu + chaperone that evolved early in the plant lineage by an alternative-splicing event of the pre-mRNA encoding the chloroplast P-type ATPase in Arabidopsis 1 (PAA1). In several land plants, recent duplication events created a separate chaperone-encoding gene coincident with loss of alternative splicing. The plant-specific Cu + chaperone delivers Cu + with specificity for PAA1, which is flipped in the envelope relative to prototypical bacterial ATPases, compatible with a role in Cu + import into the stroma and consistent with the canonical catalytic mechanism of these enzymes. The ubiquity of the chaperone suggests conservation of this Cu + -delivery mechanism and provides a unique snapshot into the evolution of a Cu + distribution pathway. We also provide evidence for an interaction between PAA2, the Cu + -ATPase in thylakoids, and the Cu + -chaperone for Cu/Zn superoxide dismutase (CCS), uncovering a Cu + network that has evolved to fine-tune Cu + distribution.Cu-transfer | inner envelope | metal transporter | Arabidopsis thaliana | Atx1

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Section: Atx1mentioning

confidence: 99%

Section: Atx1mentioning

confidence: 99%

Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis

Blaby‐Haas¹,

Padilla‐Benavides

Stübe³

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…25,27,40,42 In addition, P 1B -ATPases and also some other P-type ATPases have additional domains at their termini that are likely to have regulatory functions. 43 , but unlike P 1A -ATPases they seemingly have no associated subunits.…”

Section: Introductionmentioning

confidence: 99%

Structure and Function of Cu(I)- and Zn(II)-ATPases

et al. 2015

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Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.

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“…The role of the HMBD of P IB -ATPases is puzzling 11,26,27 . In Cu + -ATPases, a platform formed by an amphipathic helix MB' at the intracellular membrane interface (Fig.…”

mentioning

confidence: 99%

“…However, as no equivalent chaperones are known for zinc, the metal is most likely delivered by chelators such as glutathione, rendering the HMBD the most likely interaction candidate for the MB' platform in ZntA. Using a known structure of the almost identical HMBD of EcZntA 13 , the ClusPro docking server docks the domain immediately at MB', stabilized by charge complementation (as was also proposed for CopA 27,28 ) with the metal-binding CXXC-motif solvent-accessible in the vicinity of the entry funnel (Extended Data Fig. 8b-d).…”

mentioning

confidence: 99%

Structure and mechanism of Zn2+-transporting P-type ATPases

Wang

Sitsel

Meloni

et al. 2014

Nature

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106

171

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Zinc is an essential micronutrient for all living organisms, required for signaling and proper function of a range of proteins involved in e.g. DNA-binding and enzymatic catalysis 1 . In prokaryotes and photosynthetic eukaryotes Zn 2+ -transporting P-type ATPases of class IB (ZntA) are crucial for cellular redistribution and detoxification of Zn 2+ and related elements 2,3 . Here we present crystal structures representing the phosphoenzyme ground state (E2P) and a dephosphorylation intermediate (E2.P i ) of ZntA from Shigella sonnei, determined at 3.2 and 2.7 Å resolution, respectively. The structures reveal a similar fold as the Cu + -ATPases with an amphipathic helix at the membrane interface. A conserved electronegative funnel connects this region to the intramembranous high-affinity ion-binding site and may promote specific uptake of cellular Zn 2+ ions. The E2P structure displays a wide extracellular release pathway reaching the invariant residues at the high-affinity site, including Cys392, Cys394 and Asp714. The pathway closes in the E2.P i state where Asp714 interacts with the conserved Lys693, which possibly stimulates Zn 2+ release as a built-in counter-ion, as also proposed for H + -ATPases. Indeed, transport studies in liposomes provide experimental support for ZntA activity without counter-

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On Allosteric Modulation of P-Type Cu+-ATPases

Cited by 30 publications

References 74 publications

Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis

Evolution of a plant-specific copper chaperone family for chloroplast copper homeostasis

Structure and Function of Cu(I)- and Zn(II)-ATPases

Structure and mechanism of Zn2+-transporting P-type ATPases

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