6SBB

Structure of type II terpene cyclase MstE from Scytonema (apo)

6SBB の概要

• エントリーDOI: 10.2210/pdb6sbb/pdb
• 分子名称: MstE, DI(HYDROXYETHYL)ETHER, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE, ... (5 entities in total)
• 機能のキーワード: type ii terpene cyclase, marine drugs, merosterol, alpha6-alpha6 barrel, biosynthetic protein
• 由来する生物種: Scytonema sp. PCC 10023
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81695.29

構造登録者

Moosmann, P.,Ecker, F.,Leopold-Messer, S.,Cahn, J.K.B.,Groll, M.,Piel, J. (登録日: 2019-07-19, 公開日: 2020-07-15, 最終更新日: 2024-01-24)

主引用文献

Moosmann, P.,Ecker, F.,Leopold-Messer, S.,Cahn, J.K.B.,Dieterich, C.L.,Groll, M.,Piel, J.
A monodomain class II terpene cyclase assembles complex isoprenoid scaffolds.
Nat.Chem., 12:968-972, 2020

PubMed Abstract: Class II terpene cyclases, such as oxidosqualene and squalene-hopene cyclases, catalyse some of the most complex polycyclization reactions. They minimally exhibit a β,γ-didomain architecture that has been evolutionarily repurposed in a wide range of terpene-processing enzymes and likely resulted from a fusion of unidentified monodomain proteins. Although single domain class I terpene cyclases have already been identified, the corresponding class II counterparts have not been previously reported. Here we present high-resolution X-ray structures of a monodomain class II cyclase, merosterolic acid synthase (MstE). With a minimalistic β-domain architecture, this cyanobacterial enzyme is able to construct four rings in cytotoxic meroterpenoids with a sterol-like topology. The structures with bound substrate, product, and inhibitor provide detailed snapshots of a cyclization mechanism largely governed by residues located in a noncanonical enzyme region. Our results complement the few known class II cyclase crystal structures, while also indicating that archaic monodomain cyclases might have already catalyzed complex reaction cascades.

PubMed: 32778689
DOI: 10.1038/s41557-020-0515-3

実験手法

X-RAY DIFFRACTION (1.95 Å)