ArticleACS chemical biology2016
Structure and Function of Fusicoccadiene Synthase, a Hexameric Bifunctional Diterpene Synthase.
Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 77 citations in OpenAlex.
- Article
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- 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
- Structure of bifunctional variediene synthase yields unique insight on biosynthetic diterpene assembly and cyclization.Nature communications · 2025Article
- Cloning and functional characterization of sesquiterpene synthase genes from Inonotus obliquus using a Saccharomyces cerevisiae expression system.World journal of microbiology & biotechnology · 2025Article
- Structure and Function of Sabinene Synthase, a Monoterpene Cyclase That Generates a Highly Strained [3.1.0] Bicyclic Product.Biochemistry · 2024Article
- Engineering substrate channeling in a bifunctional terpene synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Engineering Substrate Channeling in Assembly-Line Terpene Biosynthesis.bioRxiv : the preprint server for biology · 2024Article
- Structure of the prenyltransferase in bifunctional copalyl diphosphate synthase from Penicillium fellutanum reveals an open hexamer conformation.Journal of structural biology · 2024Article
- Methods for the preparation and analysis of a bifunctional class II diterpene synthase, copalyl diphosphate synthase from Penicillium fellutanum.Methods in enzymology · 2024Article
- Methods for the preparation and analysis of the diterpene cyclase fusicoccadiene synthase.Methods in enzymology · 2024Article
- Structural and functional investigations of syn-copalyl diphosphate synthase from Oryza sativa.Communications chemistry · 2023Article
- Molecular insights into the catalytic promiscuity of a bacterial diterpene synthase.Nature communications · 2023Article
- Engineering a universal and efficient platform for terpenoid synthesis in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Transient Prenyltransferase-Cyclase Association in Fusicoccadiene Synthase, an Assembly-Line Terpene Synthase.Biochemistry · 2022Article
- Structure of the Repurposed Fungal Terpene Cyclase FlvF Implicated in the C-N Bond-Forming Reaction of Flavunoidine Biosynthesis.Biochemistry · 2022Article
- Discovery of non-squalene triterpenes.Nature · 2022Article
- Mechanism of the Bifunctional Multiple Product Sesterterpene Synthase AcAS from Aspergillus calidoustus.Angewandte Chemie (International ed. in English) · 2022Article
- Biosynthesis of Terpenoid-Pyrrolobenzoxazine Hybrid Natural Product CJ-12662.Angewandte Chemie (International ed. in English) · 2022Article
- Visualizing transiently associated catalytic domains in assembly-line biosynthesis using cryo-electron microscopy.Journal of structural biology · 2021Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Fusicoccin A is a diterpene glucoside phytotoxin generated by the fungal pathogen Phomopsis amygdali that causes the plant disease constriction canker, first discovered in New Jersey peach orchards in the 1930s. Fusicoccin A is also an emerging new lead in cancer chemotherapy. The hydrocarbon precursor of fusicoccin A is the tricyclic diterpene fusicoccadiene, which is generated by a bifunctional terpenoid synthase. Here, we report X-ray crystal structures of the individual catalytic domains of fusicoccadiene synthase: the C-terminal domain is a chain elongation enzyme that generates geranylgeranyl diphosphate, and the N-terminal domain catalyzes the cyclization of geranylgeranyl diphosphate to form fusicoccadiene. Crystal structures of each domain complexed with bisphosphonate substrate analogues suggest that three metal ions and three positively charged amino acid side chains trigger substrate ionization in each active site. While in vitro incubations reveal that the cyclase domain can utilize farnesyl diphosphate and geranyl diphosphate as surrogate substrates, these shorter isoprenoid diphosphates are mainly converted into acyclic alcohol or hydrocarbon products. Gel filtration chromatography and analytical ultracentrifugation experiments indicate that full-length fusicoccadiene synthase adopts hexameric quaternary structure, and small-angle X-ray scattering data yield a well-defined molecular envelope illustrating a plausible model for hexamer assembly.
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