ArticleProceedings of the National Academy of Sciences of the United States of America2013
Use of anion-aromatic interactions to position the general base in the ketosteroid isomerase active site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 66 citations in OpenAlex.
- Catalytic Promiscuity and Cascade Reaction Mechanism of Ketosteroid Isomerases for Addition Reactions of Cyclic Enones.Nature communications · 2026Article
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- Anion Recognition-Directed Supramolecular Catalysis with Functional Macrocycles and Molecular Cages.Accounts of chemical research · 2024Article
- Engineering a cleaved, prefusion-stabilized influenza B virus hemagglutinin by identification and locking of all six pH switches.PNAS nexus · 2024Article
- Design, synthesis, docking studies and bioactivity evaluation of 1,2,3-triazole eugenol derivatives.Future medicinal chemistry · 2024Article
- Tailoring Carbon Tails of Ligands on AuJournal of the American Chemical Society · 2023Article
- Molecular basis for selective uptake and elimination of organic anions in the kidney by OAT1.Nature structural & molecular biology · 2023Article
- The Realm of Unconventional Noncovalent Interactions in Proteins: Their Significance in Structure and Function.ACS omega · 2023Review
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- Mining anion-aromatic interactions in the Protein Data Bank.Chemical science · 2022Article
- Anion-π Catalysis Enabled by the Mechanical Bond.Angewandte Chemie (International ed. in English) · 2022Article
- Assessment of enzyme active site positioning and tests of catalytic mechanisms through X-ray-derived conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- E1784K, the most common Brugada syndrome and long-QT syndrome type 3 mutant, disrupts sodium channel inactivation through two separate mechanisms.The Journal of general physiology · 2020Article
- Impact of Homologous Resistance Mutations from Pathogenic Yeast on Saccharomyces cerevisiae Lanosterol 14α-Demethylase.Antimicrobial agents and chemotherapy · 2018Article
- Rapid assessment of conformational preferences in biaryl and aryl carbonyl fragments.PloS one · 2018Article
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- Measuring inter-protein pairwise interaction energies from a single native mass spectrum by double-mutant cycle analysis.Nature communications · 2017Article
- Systematic Functional Analysis of Active-Site Residues in l-Threonine Dehydrogenase fromACS omega · 2017Article
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- X-ray Structure Analysis of Indazolium trans-[Tetrachlorobis(1H-indazole)ruthenate(III)] (KP1019) Bound to Human Serum Albumin Reveals Two Ruthenium Binding Sites and Provides Insights into the Drug Binding Mechanism.Journal of medicinal chemistry · 2016Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Although the cation-pi pair, formed between a side chain or substrate cation and the negative electrostatic potential of a pi system on the face of an aromatic ring, has been widely discussed and has been shown to be important in protein structure and protein-ligand interactions, there has been little discussion of the potential structural and functional importance in proteins of the related anion-aromatic pair (i.e., interaction of a negatively charged group with the positive electrostatic potential on the ring edge of an aromatic group). We posited, based on prior structural information, that anion-aromatic interactions between the anionic Asp general base and Phe54 and Phe116 might be used instead of a hydrogen-bond network to position the general base in the active site of ketosteroid isomerase from Comamonas testosteroni as there are no neighboring hydrogen-bonding groups. We have tested the role of the Phe residues using site-directed mutagenesis, double-mutant cycles, and high-resolution X-ray crystallography. These results indicate a catalytic role of these Phe residues. Extensive analysis of the Protein Data Bank provides strong support for a catalytic role of these and other Phe residues in providing anion-aromatic interactions that position anionic general bases within enzyme active sites. Our results further reveal a potential selective advantage of Phe in certain situations, relative to more traditional hydrogen-bonding groups, because it can simultaneously aid in the binding of hydrophobic substrates and positioning of a neighboring general base.
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