6VYD

Terpenoid Cyclase FgGS in Complex with Mg, Inorganic Pyrophosphate, and Benzyltriethylammonium cation

Summary for 6VYD

• Entry DOI: 10.2210/pdb6vyd/pdb
• Descriptor: Terpenoid cyclase FgGS, MAGNESIUM ION, SULFATE ION, ... (9 entities in total)
• Functional Keywords: terpene, terpenoid, terpenoid cyclase, lyase
• Biological source: Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus)
• Total number of polymer chains: 2
• Total formula weight: 74998.16

Authors

Herbst-Gervasoni, C.J.,Christianson, D.W. (deposition date: 2020-02-26, release date: 2020-07-08, Last modification date: 2024-11-13)

Primary citation

He, H.,Bian, G.,Herbst-Gervasoni, C.J.,Mori, T.,Shinsky, S.A.,Hou, A.,Mu, X.,Huang, M.,Cheng, S.,Deng, Z.,Christianson, D.W.,Abe, I.,Liu, T.
Discovery of the cryptic function of terpene cyclases as aromatic prenyltransferases.
Nat Commun, 11:3958-3958, 2020

PubMed Abstract: Catalytic versatility is an inherent property of many enzymes. In nature, terpene cyclases comprise the foundation of molecular biodiversity as they generate diverse hydrocarbon scaffolds found in thousands of terpenoid natural products. Here, we report that the catalytic activity of the terpene cyclases AaTPS and FgGS can be switched from cyclase to aromatic prenyltransferase at basic pH to generate prenylindoles. The crystal structures of AaTPS and FgGS provide insights into the catalytic mechanism of this cryptic function. Moreover, aromatic prenyltransferase activity discovered in other terpene cyclases indicates that this cryptic function is broadly conserved among the greater family of terpene cyclases. We suggest that this cryptic function is chemoprotective for the cell by regulating isoprenoid diphosphate concentrations so that they are maintained below toxic thresholds.

PubMed: 32769971
DOI: 10.1038/s41467-020-17642-2

Experimental method

X-RAY DIFFRACTION (1.46 Å)