ArticleProtein science : a publication of the Protein Society1997
Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions.
Article in Protein science : a publication of the Protein Society, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Transient Absorption Spectroscopy of Blue Copper Sites in Divergent Protein Folds: Azurin Versus Multicopper Oxidase.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Suppression of mitochondrial energy production by a photosynthetic bacterial cupredoxin peptide inhibits tumor growth.Signal transduction and targeted therapy · 2026Article
- Elevated temperature simulating heatwaves restructures active nitrifying communities and associated viruses in tidal flats and agricultural soils.The ISME journal · 2026Article
- The structure of plastocyanin tunes the midpoint potential by restricting axial ligation of the reduced copper ion.Communications chemistry · 2023Article
- Molecular Docking of Lac_CB10: Highlighting the Great Potential for Bioremediation of Recalcitrant Chemical Compounds by One Predicted Bacteroidetes CopA-Laccase.International journal of molecular sciences · 2023Article
- Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- New putative phenol oxidase in ascidian blood cells.Scientific reports · 2022Article
- Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis.Acta crystallographica. Section D, Structural biology · 2021Article
- A structural-chemical explanation of fungal laccase activity.Scientific reports · 2018Article
- Article
- The Rise of Radicals in Bioinorganic Chemistry.Israel journal of chemistry · 2016Article
- Nitrite Reductase Activity in Engineered Azurin Variants.Inorganic chemistry · 2016Article
- The CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding Proteins.Biochemistry · 2016Article
- X-ray-induced catalytic active-site reduction of a multicopper oxidase: structural insights into the proton-relay mechanism and O2-reduction states.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Blood Clotting Factor VIII: From Evolution to Therapy.Acta naturae · 2013Article
- Phylogenetic analysis of six-domain multi-copper blue proteins.PLoS currents · 2013Article
- Incorporation of the red copper nitrosocyanin binding loop into blue copper azurin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- The Laccase Engineering Database: a classification and analysis system for laccases and related multicopper oxidases.Database : the journal of biological databases and curation · 2011Article
- Laccases: a never-ending story.Cellular and molecular life sciences : CMLS · 2010Review
- Multicopper oxidases: a workshop on copper coordination chemistry, electron transfer, and metallophysiology.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2010Review
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Authors and funding
3 authors.
Funding
Abstract
The three-dimensional structures of the copper-containing enzymes ascorbate oxidase, ceruloplasmin, and nitrite reductase, comprised of multiple domains with a cupredoxin fold, are consistent with having evolved from a common ancestor. The presence or absence of copper sites has complicated ascertaining the structural and evolutionary relationship among these and related proteins. Simultaneous structural superposition of the enzyme domains and their known cupredoxin relatives shows clearly that there are at least six cupredoxin classes, and that the evolution of the conserved core of these domains is independent of the presence or absence of copper sites. Relationships among the variable loops in these structures show that the two-domain ancestor of the blue oxidases contained a trinuclear-copper interface but could not have functioned in a monomeric state. Comparison of the sequence of the copper-containing, iron-regulating protein. Ferrous transport (Fet3) from yeast to the structurally defined core and loop residues of the cupredoxins suggests specific residues that could be involved in the ferroxidase activity of Fet3.
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