ArticleNature communications2021
Structural insight on assembly-line catalysis in terpene biosynthesis.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 43 citations in OpenAlex.
- 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
- Structural insights into a bacterial terpene cyclase fused with haloacid Dehalogenase-like phosphatase.Chemical science · 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
- Structure of bifunctional variediene synthase yields unique insight on biosynthetic diterpene assembly and cyclization.Nature communications · 2025Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.Nature communications · 2024Article
- Engineering substrate channeling in a bifunctional terpene synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell.bioRxiv : the preprint server for biology · 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 the diterpene cyclase fusicoccadiene synthase.Methods in enzymology · 2024Article
- Structural basis of a transcription pre-initiation complex on a divergent promoter.Molecular cell · 2023Article
- Chaga mushroom triterpenoids as adjuncts to minimally invasive cancer therapies: A review.Current research in toxicology · 2023Article
- Novel Sesquiterpene and Diterpene Aminoglycosides from the Deep-Sea-Sediment FungusMarine drugs · 2022Article
- Transient Prenyltransferase-Cyclase Association in Fusicoccadiene Synthase, an Assembly-Line Terpene Synthase.Biochemistry · 2022Article
- Design and Characterization of In-One Protease-Esterase PluriZyme.International journal of molecular sciences · 2022Article
- A Plurizyme with Transaminase and Hydrolase Activity Catalyzes Cascade Reactions.Angewandte Chemie (International ed. in English) · 2022Article
- Discovery and analysis of a new class of triterpenes derived from hexaprenyl pyrophosphate.Engineering microbiology · 2022Article
- Discovery of non-squalene triterpenes.Nature · 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
7 authors at 1 institution in 1 country.
Funding
Abstract
Fusicoccadiene synthase from Phomopsis amygdali (PaFS) is a unique bifunctional terpenoid synthase that catalyzes the first two steps in the biosynthesis of the diterpene glycoside Fusicoccin A, a mediator of 14-3-3 protein interactions. The prenyltransferase domain of PaFS generates geranylgeranyl diphosphate, which the cyclase domain then utilizes to generate fusicoccadiene, the tricyclic hydrocarbon skeleton of Fusicoccin A. Here, we use cryo-electron microscopy to show that the structure of full-length PaFS consists of a central octameric core of prenyltransferase domains, with the eight cyclase domains radiating outward via flexible linker segments in variable splayed-out positions. Cryo-electron microscopy and chemical crosslinking experiments additionally show that compact conformations can be achieved in which cyclase domains are more closely associated with the prenyltransferase core. This structural analysis provides a framework for understanding substrate channeling, since most of the geranylgeranyl diphosphate generated by the prenyltransferase domains remains on the enzyme for cyclization to form fusicoccadiene.
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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.