ArticleJournal of the American Chemical Society2016
A Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed Metalloproteins.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Design of a site selective heterochromic bimetallic lanthanide coiled coil with nanometre-scale control.Chemical science · 2026Article
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- Breaking symmetry: Metal-guided assembly of heterotrimeric coiled coils.Methods in enzymology · 2025Article
- Human Retrotransposons and Effective Computational Detection Methods for Next-Generation Sequencing Data.Life (Basel, Switzerland) · 2022Review
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Cu(I) Binding to Designed Proteins Reveals a Putative Copper Binding Site of the Human Line1 Retrotransposon Protein ORF1p.Inorganic chemistry · 2022Article
- Rational design of photosynthetic reaction center protein maquettes.Frontiers in molecular biosciences · 2022Article
- Location-Dependent Lanthanide Selectivity Engineered into Structurally Characterized Designed Coiled Coils.Angewandte Chemie (International ed. in English) · 2021Article
- Open Reading Frame 1 Protein of the Human Long Interspersed Nuclear Element 1 Retrotransposon Binds Multiple Equivalents of Lead.Journal of the American Chemical Society · 2021Article
- Making or Breaking Metal-Dependent Catalytic Activity: The Role of Stammers in Designed Three-Stranded Coiled Coils.Angewandte Chemie (International ed. in English) · 2020Article
- Catalysis and Electron Transfer in De Novo Designed Helical Scaffolds.Angewandte Chemie (International ed. in English) · 2020Review
- Heteromeric three-stranded coiled coils designed using a Pb(II)(Cys)Nature chemistry · 2020Article
- Noncoded Amino Acids in de Novo Metalloprotein Design: Controlling Coordination Number and Catalysis.Accounts of chemical research · 2019Article
- How Outer Coordination Sphere Modifications Can Impact Metal Structures in Proteins: A Crystallographic Evaluation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go.ACS catalysis · 2018Article
- Modifying the Steric Properties in the Second Coordination Sphere of Designed Peptides Leads to Enhancement of Nitrite Reductase Activity.Angewandte Chemie (International ed. in English) · 2018Article
- Article
- Incorporation of second coordination sphere D-amino acids alters Cd(II) geometries in designed thiolate-rich proteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Metal Substitution and Solvomorphism in Alkylthiolate-Bridged ZnACS omega · 2017Article
- d-Cysteine Ligands Control Metal Geometries within De Novo Designed Three-Stranded Coiled Coils.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
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4 authors.
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Abstract
Preorganization and predisposition are important molecular recognition concepts exploited by nature to obtain site-specific and selective metal binding to proteins. While native structures containing an MS3 core are often unavailable in both apo- and holo-forms, one can use designed three-stranded coiled coils (3SCCs) containing tris-thiolate sites to evaluate these concepts. We show that the preferred metal geometry dictates the degree to which the cysteine rotamers change upon metal complexation. The Cys ligands in the apo-form are preorganized for binding trigonal pyramidal species (Pb(II)S3 and As(III)S3) in an endo conformation oriented toward the 3SCC C-termini, whereas the cysteines are predisposed for trigonal planar Hg(II)S3 and 4-coordinate Zn(II)S3O structures, requiring significant thiol rotation for metal binding. This study allows assessment of the importance of protein fold and side-chain reorientation for achieving metal selectivity in human retrotransposons and metalloregulatory proteins.
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