ArticleThe Journal of biological chemistry2007
Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- Cu Homeostasis in Bacteria: The Ins and Outs.Membranes · 2020Review
- Article
- CopR, a Global Regulator of Transcription to Maintain Copper Homeostasis inFrontiers in microbiology · 2020Article
- Unique roles of iron and zinc binding to the yeast Fe-S cluster scaffold assembly protein "Isu1".Metallomics : integrated biometal science · 2019Article
- TheProceedings of the National Academy of Sciences of the United States of America · 2019Article
- A comprehensive phylogenetic analysis of copper transporting PMicrobiologyOpen · 2017Article
- In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation.Metallomics : integrated biometal science · 2017Article
- Bacterial Cu(+)-ATPases: models for molecular structure-function studies.Metallomics : integrated biometal science · 2016Review
- Cleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe-2S cluster.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The mechanism of Cu+ transport ATPases: interaction with CU+ chaperones and the role of transient metal-binding sites.The Journal of biological chemistry · 2013Article
- The structure of the BfrB-Bfd complex reveals protein-protein interactions enabling iron release from bacterioferritin.Journal of the American Chemical Society · 2012Article
- The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2011Article
- Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly.Biochemistry · 2010Article
- Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA.Proteins · 2010Article
- Copper metallochaperones.Annual review of biochemistry · 2010Review
- Structural organization of human Cu-transporting ATPases: learning from building blocks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Review
- Interaction between cyanobacterial copper chaperone Atx1 and zinc homeostasis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Article
- Structural biology of copper trafficking.Chemical reviews · 2009Review
- Chaperone-mediated Cu+ delivery to Cu+ transport ATPases: requirement of nucleotide binding.The Journal of biological chemistry · 2009Article
- Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are homologous to the human Wilson and Menkes disease proteins. The genome of the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper chaperone that contains an unusual cysteine-rich N-terminal domain of 130 amino acids in addition to a C-terminal copper binding domain with a conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to proteins found only in extremophiles and is the only such protein that is fused to a copper chaperone. Surprisingly, optical, electron paramagnetic resonance, and x-ray absorption spectroscopic data indicate the presence of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper ions, one in each domain. The 1.8 A resolution crystal structure of CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold and that the protein also binds a zinc ion at a four-cysteine site. CopZ can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain and is capable of reducing Cu2+ to Cu+. This unique fusion of a redox-active domain with a CXXC-containing copper chaperone domain is relevant to the evolution of copper homeostatic mechanisms and suggests new models for copper trafficking.
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