ArticleBiochemistry2010
Structure of epi-isozizaene synthase from Streptomyces coelicolor A3(2), a platform for new terpenoid cyclization templates.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
73 citing papers in PubMed, 156 citations in OpenAlex.
- Divergent Lineage of Terpene Synthases Establishes Terpenoid Biosynthesis in Brown Macroalgae.Journal of the American Chemical Society · 2026Article
- Designed Water Capture in Terpene Synthase Catalysis.Chembiochem : a European journal of chemical biology · 2026Article
- Structure and Mechanism of Avermitilol Synthase, a Sesquiterpene Cyclase That Generates a Highly Strained 6-6-3 Tricyclic Alcohol.Biochemistry · 2025Article
- Crystal structure and catalytic mechanism of drimenol synthase, an unusual bifunctional terpene cyclase-phosphatase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genome Mining of Terpene Synthases from FourteenMicroorganisms · 2025Article
- Engineering terpene synthases and their substrates for the biocatalytic production of terpene natural products and analogues.Chemical communications (Cambridge, England) · 2025Review
- Molecular insights into a distinct class of terpenoid cyclases.Nature communications · 2025Article
- Structure and Function of Sabinene Synthase, a Monoterpene Cyclase That Generates a Highly Strained [3.1.0] Bicyclic Product.Biochemistry · 2024Article
- Single Point Mutation Abolishes Water Capture in Germacradien-4-ol Synthase.Chembiochem : a European journal of chemical biology · 2024Article
- Structure-Based Engineering of a Sesquiterpene Cyclase to Generate an Alcohol Product: Conversion ofBiochemistry · 2024Article
- Decoding Catalysis by Terpene Synthases.ACS catalysis · 2023Review
- Genomic Based Analysis of the Biocontrol SpeciesJournal of fungi (Basel, Switzerland) · 2023Article
- Reprogramming the Cyclization Cascade ofBiochemistry · 2023Article
- Tryptophan Stabilization of a Biochemical Carbocation Evaluated by Analysis of π Complexes of 3-Ethylindole with theACS omega · 2023Article
- Molecular insights into the catalytic promiscuity of a bacterial diterpene synthase.Nature communications · 2023Article
- Actinomycetes as Producers of Biologically Active Terpenoids: Current Trends and Patents.Pharmaceuticals (Basel, Switzerland) · 2023Review
- How a 10-ACS catalysis · 2022Article
- Identification and Characterization of Bifunctional Drimenol Synthases of Marine Bacterial Origin.ACS chemical biology · 2022Article
- Molecular Determinants of Carbocation Cyclisation in Bacterial Monoterpene Synthases.Chembiochem : a European journal of chemical biology · 2022Article
- Mining methods and typical structural mechanisms of terpene cyclases.Bioresources and bioprocessing · 2021Review
13 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The X-ray crystal structure of recombinant epi-isozizaene synthase (EIZS), a sesquiterpene cyclase from Streptomyces coelicolor A3(2), has been determined at 1.60 A resolution. Specifically, the structure of wild-type EIZS is that of its closed conformation in complex with three Mg(2+) ions, inorganic pyrophosphate (PP(i)), and the benzyltriethylammonium cation (BTAC). Additionally, the structure of D99N EIZS has been determined in an open, ligand-free conformation at 1.90 A resolution. Comparison of these two structures provides the first view of conformational changes required for substrate binding and catalysis in a bacterial terpenoid cyclase. Moreover, the binding interactions of BTAC may mimic those of a carbocation intermediate in catalysis. Accordingly, the aromatic rings of F95, F96, and F198 appear to be well-oriented to stabilize carbocation intermediates in the cyclization cascade through cation-pi interactions. Mutagenesis of aromatic residues in the enzyme active site results in the production of alternative sesquiterpene product arrays due to altered modes of stabilization of carbocation intermediates as well as altered templates for the cyclization of farnesyl diphosphate. Accordingly, the 1.64 A resolution crystal structure of F198A EIZS in a complex with three Mg(2+) ions, PP(i), and BTAC reveals an alternative binding orientation of BTAC; alternative binding orientations of a carbocation intermediate could lead to the formation of alternative products. Finally, the crystal structure of wild-type EIZS in a complex with four Hg(2+) ions has been determined at 1.90 A resolution, showing that metal binding triggers a significant conformational change of helix G to cap the active site.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.