ArticleJournal of the American Chemical Society2016
Structure of the ent-Copalyl Diphosphate Synthase PtmT2 from Streptomyces platensis CB00739, a Bacterial Type II Diterpene Synthase.
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 35 papers.
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35 citing papers in PubMed, 62 citations in OpenAlex.
- Investigating conserved aromatic residues in ent-copalyl pyrophosphate synthases required for gibberellin phytohormone biosynthesis.Phytochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.Biochemistry · 2025Article
- Cryo-EM Structure of the Cyclase Domain and Evaluation of Substrate Channeling in a Bifunctional Class II Terpene Synthase.bioRxiv : the preprint server for biology · 2025Article
- Discovery of bacterial terpenoids by genome mining.Methods in enzymology · 2025Article
- Class II terpene cyclases: structures, mechanisms, and engineering.Natural product reports · 2024Review
- Methods for the preparation and analysis of a bifunctional class II diterpene synthase, copalyl diphosphate synthase from Penicillium fellutanum.Methods in enzymology · 2024Article
- Extending the Structural Diversity of Labdane Diterpenoids from Marine-Derived FungusMarine drugs · 2023Article
- Structural and functional investigations of syn-copalyl diphosphate synthase from Oryza sativa.Communications chemistry · 2023Article
- Actinomycetes as Producers of Biologically Active Terpenoids: Current Trends and Patents.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Discovery, Structure, and Mechanism of a Class II Sesquiterpene Cyclase.Journal of the American Chemical Society · 2022Article
- Mutation of the eunicellane synthase Bnd4 alters its product profile and expands its prenylation ability.Organic & biomolecular chemistry · 2022Article
- Structure-guided product determination of the bacterial type II diterpene synthase Tpn2.Communications chemistry · 2022Article
- Investigation of Acid-Base Catalysis in Halimadienyl Diphosphate Synthase Involved inACS bio & med chem Au · 2022Article
- Thermoadaptation in an Ancestral Diterpene Cyclase by Altered Loop Stability.The journal of physical chemistry. B · 2022Article
- Identification and Characterization of Bifunctional Drimenol Synthases of Marine Bacterial Origin.ACS chemical biology · 2022Article
- Efficient production of clerodane andBeilstein journal of organic chemistry · 2022Article
- Engineering the Prenyltransferase Domain of a Bifunctional Assembly-Line Terpene Synthase.Biochemistry · 2021Article
- Mechanistic Insights into the Formation of the 6,10-Bicyclic Eunicellane Skeleton by the Bacterial Diterpene Synthase Bnd4.Angewandte Chemie (International ed. in English) · 2021Article
- Functional characterization and structural bases of two class I diterpene synthases in pimarane-type diterpene biosynthesis.Communications chemistry · 2021Article
- Mining methods and typical structural mechanisms of terpene cyclases.Bioresources and bioprocessing · 2021Review
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12 authors at 4 institutions in 1 country.
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Abstract
Terpenoids are the largest and most structurally diverse family of natural products found in nature, yet their presence in bacteria is underappreciated. The carbon skeletons of terpenoids are generated through carbocation-dependent cyclization cascades catalyzed by terpene synthases (TSs). Type I and type II TSs initiate cyclization via diphosphate ionization and protonation, respectively, and protein structures of both types are known. Most plant diterpene synthases (DTSs) possess three α-helical domains (αβγ), which are thought to have arisen from the fusion of discrete, ancestral bacterial type I TSs (α) and type II TSs (βγ). Type II DTSs of bacterial origin, of which there are no structurally characterized members, are a missing piece in the structural evolution of TSs. Here, we report the first crystal structure of a type II DTS from bacteria. PtmT2 from Streptomyces platensis CB00739 was verified as an ent-copalyl diphosphate synthase involved in the biosynthesis of platensimycin and platencin. The crystal structure of PtmT2 was solved at a resolution of 1.80 Å, and docking studies suggest the catalytically active conformation of geranylgeranyl diphosphate (GGPP). Site-directed mutagenesis confirmed residues involved in binding the diphosphate moiety of GGPP and identified DxxxxE as a potential Mg(2+)-binding motif for type II DTSs of bacterial origin. Finally, both the shape and physicochemical properties of the active sites are responsible for determining specific catalytic outcomes of TSs. The structure of PtmT2 fundamentally advances the knowledge of bacterial TSs, their mechanisms, and their role in the evolution of TSs.
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