7XQ4

Drimenyl diphosphate synthase from Streptomyces showdoensis (apo)

7XQ4 の概要

• エントリーDOI: 10.2210/pdb7xq4/pdb
• 分子名称: SQHop_cyclase_C domain-containing protein (2 entities in total)
• 機能のキーワード: terpene synthases, type ii tss, biosynthetic protein
• 由来する生物種: Streptomyces showdoensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55088.17

構造登録者

Pan, X.M.,Du, W.Y.,Yang, Q.,Zhang, B.,Dong, L.B. (登録日: 2022-05-06, 公開日: 2023-03-15, 最終更新日: 2024-04-03)

主引用文献

Pan, X.,Du, W.,Zhang, X.,Lin, X.,Li, F.R.,Yang, Q.,Wang, H.,Rudolf, J.D.,Zhang, B.,Dong, L.B.
Discovery, Structure, and Mechanism of a Class II Sesquiterpene Cyclase.
J.Am.Chem.Soc., 144:22067-22074, 2022

PubMed Abstract: Terpene cyclases (TCs), extraordinary enzymes that create the structural diversity seen in terpene natural products, are traditionally divided into two classes, class I and class II. Although the structural and mechanistic features of class I TCs are well-known, the corresponding details in class II counterparts have not been fully characterized. Here, we report the genome mining discovery and structural characterization of two class II sesquiterpene cyclases (STCs) from . These drimenyl diphosphate synthases (DMSs) are the first STCs shown to possess β,γ-didomain architecture. High-resolution X-ray crystal structures of DMS from (SsDMS) in complex with both a farnesyl diphosphate and Mg unveiled an induced-fit mechanism, with an unprecedented Mg binding mode, finally solving one of the lingering questions in class II TC enzymology. This study supports continued genome mining for novel bacterial TCs and provides new mechanistic insights into canonical class II TCs that will lead to advances in TC engineering and synthetic biology.

PubMed: 36416740
DOI: 10.1021/jacs.2c09412

実験手法

X-RAY DIFFRACTION (1.58 Å)