ArticleBiochemistry2015
Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- A De Novo Designed Metalloprotein Displays Variable Thermal Stability and Binding Stoichiometry with Transition Metal Ions.Chembiochem : a European journal of chemical biology · 2025Article
- Incorporation of a molybdenum atom in a Rubredoxin-type Centre of a de novo-designed αJournal of inorganic biochemistry · 2023Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- De novo metalloprotein design.Nature reviews. Chemistry · 2022Article
- Recent advances in bacterial biosensing and bioremediation of cadmium pollution: a mini-review.World journal of microbiology & biotechnology · 2021Review
- Nitrite reductase activity within an antiparallel de novo scaffold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Rational De Novo Design of a Cu Metalloenzyme for Superoxide Dismutation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Selective coordination of three transition metal ions within a coiled-coil peptide scaffold.Chemical science · 2019Article
- Probing Metal Ion Discrimination in a Protein Designed to Bind Uranyl Cation With Femtomolar Affinity.Frontiers in molecular biosciences · 2019Article
- Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.Inorganic chemistry · 2018Article
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- Engineering glycoside hydrolase stability by the introduction of zinc binding.Acta crystallographica. Section D, Structural biology · 2018Article
- Development of a Rubredoxin-Type Center Embedded in a de Dovo-Designed Three-Helix Bundle.Biochemistry · 2018Article
- Benchmarking a computational design method for the incorporation of metal ion-binding sites at symmetric protein interfaces.Protein science : a publication of the Protein Society · 2017Article
- Intramolecular Photogeneration of a Tyrosine Radical in a Designed Protein.ChemPhotoChem · 2017Article
- Probing the minimal determinants of zinc binding with computational protein design.Protein engineering, design & selection : PEDS · 2016Article
- Electron transfer activity of a de novo designed copper center in a three-helix bundle fold.Biochimica et biophysica acta · 2016Article
- Oxidation Protection in Metal-Binding Peptide Motif and Its Application to Antibody for Site-Selective Conjugation.PloS one · 2016Article
- Variable primary coordination environments of Cd(II) binding to three helix bundles provide a pathway for rapid metal exchange.Metallomics : integrated biometal science · 2015Article
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5 authors.
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Abstract
De novo protein design is a biologically relevant approach that provides a novel process in elucidating protein folding and modeling the metal centers of metalloproteins in a completely unrelated or simplified fold. An integral step in de novo protein design is the establishment of a well-folded scaffold with one conformation, which is a fundamental characteristic of many native proteins. Here, we report the NMR solution structure of apo α3DIV at pH 7.0, a de novo designed three-helix bundle peptide containing a triscysteine motif (Cys18, Cys28, and Cys67) that binds toxic heavy metals. The structure comprises 1067 NOE restraints derived from multinuclear multidimensional NOESY, as well as 138 dihedral angles (ψ, φ, and χ1). The backbone and heavy atoms of the 20 lowest energy structures have a root mean square deviation from the mean structure of 0.79 (0.16) Å and 1.31 (0.15) Å, respectively. When compared to the parent structure α3D, the substitution of Leu residues to Cys enhanced the α-helical content of α3DIV while maintaining the same overall topology and fold. In addition, solution studies on the metalated species illustrated metal-induced stability. An increase in the melting temperatures was observed for Hg(II), Pb(II), or Cd(II) bound α3DIV by 18-24 °C compared to its apo counterpart. Further, the extended X-ray absorption fine structure analysis on Hg(II)-α3DIV produced an average Hg(II)-S bond length at 2.36 Å, indicating a trigonal T-shaped coordination environment. Overall, the structure of apo α3DIV reveals an asymmetric distorted triscysteine metal binding site, which offers a model for native metalloregulatory proteins with thiol-rich ligands that function in regulating toxic heavy metals, such as ArsR, CadC, MerR, and PbrR.
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