Journal ArticleDOI
The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction.
Lucia Banci,Ivano Bertini,Francesca Cantini,Isabella C. Felli,Leonardo Gonnelli,Nick Hadjiliadis,Nick Hadjiliadis,Roberta Pierattelli,Antonio Rosato,Petros G. Voulgaris +9 more
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TLDR
This study structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase and provided an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners.Abstract:
Cellular systems allow transition-metal ions to reach or leave the cell or intracellular locations through metal transfer between proteins. By coupling mutagenesis and advanced NMR experiments, we structurally characterized the adduct between the copper chaperone Atx1 and the first copper(I)-binding domain of the Ccc2 ATPase. Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners.read more
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Function and Regulation of Human Copper-Transporting ATPases
TL;DR: Current data on the structural organization and functional properties of ATP7A and ATP7B as well as their localization and functions in various tissues are summarized, and the current models of regulated trafficking of human Cu-ATPases are discussed.
Journal ArticleDOI
Coordination chemistry of bacterial metal transport and sensing.
TL;DR: Metal homeostasis is governed by the formation of specific protein-metal coordination complexes used to effect uptake, efflux, intracellular trafficking within compartments, and storage, and is the focus of this review.
Journal ArticleDOI
A Cytosolic Iron Chaperone That Delivers Iron to Ferritin
TL;DR: Human poly (rC)–binding protein 1 (PCBP1) increased the amount of iron loaded into ferritin when expressed in yeast and can function as a cytosolic iron chaperone in the delivery of iron to ferrit in vitro.
Journal ArticleDOI
Affinity gradients drive copper to cellular destinations
TL;DR: This study provides the thermodynamic basis for the kinetic processes that lead to the distribution of cellular copper, and complements the finding that fast copper-transfer pathways require metal-mediated protein– protein interactions and therefore protein–protein specific recognition.
Journal ArticleDOI
Structural biology of copper trafficking.
Amie K. Boal,Amy C. Rosenzweig +1 more
TL;DR: Intracellular copper concentrations must be controlled such that copper ions are provided to essential enzymes, but do not accumulate to deleterious levels, and the same redox properties that render copper useful in all these metalloproteins can lead to oxidative damage in cells.
References
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Journal ArticleDOI
Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins.
TL;DR: The structures of Hah1 provide models for intermediates in metal ion transfer and suggest a detailed molecular mechanism for protein recognition and metal ion exchange between MT/HCXXC containing domains.
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Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1.
TL;DR: The (1)H NMR solution structure of the Cu(I)-bound form of Atx1, a 73-amino acid metallochaperone protein from the yeast Saccharomyces cerevisiae, has been determined, and a pivotal role for Lys65 in the metal capture and release process is proposed.
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Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p.
TL;DR: It is shown that apo-HAH1p can bind in vitro to copper-loaded WDp, suggesting reversibility of copper transfer from HAH 1p to WD/MNKp, and the protein-protein interaction is modeled and a theoretical representation of the HAH1P·Cu·WD/ MNKp complex is presented.
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Structure of human Wilson protein domains 5 and 6 and their interplay with domain 4 and the copper chaperone HAH1 in copper uptake
TL;DR: Human Wilson protein is a copper-transporting ATPase located in the secretory pathway possessing six N-terminal metal-binding domains, which are suggested to be two acceptors of Cu(I) from HAH1, which then somehow route copper to WLN5-6, before the ATP-driven transport of copper across the vesicular membrane.
Journal ArticleDOI
Characterization of the Binding Interface between the Copper Chaperone Atx1 and the First Cytosolic Domain of Ccc2 ATPase
Fabio Arnesano,Lucia Banci,Ivano Bertini,Francesca Cantini,Simone Ciofi-Baffoni,David L. Huffman,Thomas V. O'Halloran +6 more
TL;DR: 15N and 1H chemical shifts suggest the regions of interaction that, together with independent information, allow a structural model of the adduct to be proposed and is relevant as a structural and kinetic model for copper transfer from Atx1 to Ccc2a in physiological conditions.