Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces.
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The homoeostasis of metal ions in cells is the result of the contribution of several cellular pathways that involve transient, often weak, protein–protein interactions. Metal transfer typically implies the formation of adducts where the metal itself acts as a bridge between proteins, by co-ordinating residues of both interacting partners. In the present study we address the interaction between the human copper(I)-chaperone HAH1 (human ATX1 homologue) and a metal-binding domain in one of its partners, namely the P-type copper-transporting ATPase, ATP7A (ATPase, Cu+ transporting, α polypeptide). The adduct was structurally characterized in solution, in the presence of copper(I), and through X-ray crystallography, upon replacing copper(I) with cadmium(II). Further insight was obtained through molecular modelling techniques and site-directed mutagenesis. It was found that the interaction involves a relatively small interface (less than 1000 Å2, 1 Å=0.1 nm) with a low fraction of non-polar atoms. These observations provide a possible explanation for the low affinity of the two apoproteins. It appears that electrostatics is important in selecting which domain of the ATPase is able to form detectable amounts of the metal-mediated adduct with HAH1.
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When Ccc2 and MK1 formed hetero-complexes with their respective chaperones, helix 1 in both Ccc2 and MK1 unwinded.
“It was reported that when Ccc2 and MK1 formed hetero-complexes with their respective chaperones, helix 1 (which participates in the interface between the proteins) in both Ccc2 and MK1 unwinded [16], [30].”
From In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein (2012) · cites this paper as [16]
In “The structures of HAH1 and MNK1 within the HAH1-Cu(I)-MNK1 adduct” (page unavailable), the paper reports a reorientation of MNK1 helix 1 and cites a reported rearrangement of the same helix in yeast Ccc2a upon interaction with its partner. It does not say that helix 1 unwinds in either protein; rearrangement is less specific than the attributed claim. (LLM, conf=0.86)
Experimental — accuracy not yet measuredA number of favorable electrostatic interactions across the interface have been identified.
“A number of favorable electrostatic interactions across the interface have been identified [16], [30].”
From In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein (2012) · cites this paper as [16]
A K1 value of 10^5, similar to our result, was reported for Atox1-Cu-MK1, although this value may truly be a combination of K1 and 1/K2.
“A K1 value of 105, i.e. similar to our result, was reported for Atox1-Cu-MK1 although this value may truly be a combination of K1 and 1/K2 [16].”
From In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein (2012) · cites this paper as [16]
Based on data for the Atox1-Ccc2 and Atox1-MK1 complexes, the protein-protein interface in the hetero-complex is relatively small and involves amino acids not normally found at interfaces.
“Based on data for the Atox1-Ccc2 and Atox1-MK1 complexes, the protein-protein interface in the hetero-complex is relatively small and involves amino acids not normally found at interfaces [16].”
From In Vitro Thermodynamic Dissection of Human Copper Transfer from Chaperone to Target Protein (2012) · cites this paper as [16]
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- Authors
- Banci, L., Bertini, I., Calderone, V., Della-Malva, N., Felli, I. C., Neri, S., Pavelkova, A., & Rosato, A.
- Affiliations
- Fondazione Farmacogenomica FiorGen (IT)
- University of Florence (IT)
- Corresponding author
- Banci, Lucia
- Bertini, Ivano
- Calderone, Vito
- Neri, Sara
- Pavelkova, Anna
- Rosato, Antonio
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2009-07-29
- Volume
- 422
- Issue
- 1
- Pages
- 37-42
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1964635284
- Cited by
- 94
- References
- 44
- Citations by year
- 2026: 4 · 2024: 4 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 4 · 2019: 7 · 2018: 7 · 2017: 7 · 2016: 5 · 2015: 4 · 2014: 4 · 2013: 14 · 2012: 11
- FWCI
- 8.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Florence Research (University of Florence) (submittedVersion)
- Trinity's Access to Research Output (TARA) (Trinity College Dublin) (submittedVersion, other-oa)
- Funders
- Ente Cassa di Risparmio di Firenze
- Ministero dell’Istruzione, dell’Università e della Ricerca (PRIN2005)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- ATX1, ATP7A, metallochaperone, interaction interfaces, electrostatic interactions, metal homeostasis, cadmium substitution, metal-binding domain
- MeSH terms
- Copper-Transporting ATPases, Copper Transport Proteins, Adenosine Triphosphatases, Cadmium, Copper, Humans, Mutation, Protein Binding, Solutions, Surface Properties, Protein Serine-Threonine Kinases, Protein Structure, Tertiary, Crystallography, X-Ray, Molecular Chaperones, Cation Transport Proteins, Intracellular Signaling Peptides and Proteins, Static Electricity, Metallochaperones
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