7VTA

Talaromyces verruculosus talaropentaene synthase apo

7VTA の概要

• エントリーDOI: 10.2210/pdb7vta/pdb
• 分子名称: TvTS cyclase domain (2 entities in total)
• 機能のキーワード: talaromyces verruculosus, talaropentaene synthase, triterpene, transferase
• 由来する生物種: Talaromyces verruculosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36987.49

構造登録者

Hui, T.,Mori, T.,Abe, I. (登録日: 2021-10-28, 公開日: 2022-06-08, 最終更新日: 2023-11-29)

主引用文献

Tao, H.,Lauterbach, L.,Bian, G.,Chen, R.,Hou, A.,Mori, T.,Cheng, S.,Hu, B.,Lu, L.,Mu, X.,Li, M.,Adachi, N.,Kawasaki, M.,Moriya, T.,Senda, T.,Wang, X.,Deng, Z.,Abe, I.,Dickschat, J.S.,Liu, T.
Discovery of non-squalene triterpenes.
Nature, 606:414-419, 2022

PubMed Abstract: All known triterpenes are generated by triterpene synthases (TrTSs) from squalene or oxidosqualene. This approach is fundamentally different from the biosynthesis of short-chain (C-C) terpenes that are formed from polyisoprenyl diphosphates. In this study, two fungal chimeric class I TrTSs, Talaromyces verruculosus talaropentaene synthase (TvTS) and Macrophomina phaseolina macrophomene synthase (MpMS), were characterized. Both enzymes use dimethylallyl diphosphate and isopentenyl diphosphate or hexaprenyl diphosphate as substrates, representing the first examples, to our knowledge, of non-squalene-dependent triterpene biosynthesis. The cyclization mechanisms of TvTS and MpMS and the absolute configurations of their products were investigated in isotopic labelling experiments. Structural analyses of the terpene cyclase domain of TvTS and full-length MpMS provide detailed insights into their catalytic mechanisms. An AlphaFold2-based screening platform was developed to mine a third TrTS, Colletotrichum gloeosporioides colleterpenol synthase (CgCS). Our findings identify a new enzymatic mechanism for the biosynthesis of triterpenes and enhance understanding of terpene biosynthesis in nature.

PubMed: 35650436
DOI: 10.1038/s41586-022-04773-3

実験手法

X-RAY DIFFRACTION (2.4 Å)