8I6P

The cryo-EM structure of OsCyc1 tetramer state

8I6P の概要

• エントリーDOI: 10.2210/pdb8i6p/pdb
• EMDBエントリー: 35202
• 分子名称: Syn-copalyl diphosphate synthase, chloroplastic (1 entity in total)
• 機能のキーワード: syn-copalyl diphosphate synthase, labdane-related diterpenoids, oligomer cryo-em structure, plant defense, plant protein, isomerase
• 由来する生物種: Oryza sativa Japonica Group (Japanese rice)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 353709.78

構造登録者

Ma, X.L.,Xu, H.F.,Tong, Y.R.,Luo, Y.F.,Dong, Q.H.,Jiang, T. (登録日: 2023-01-29, 公開日: 2023-12-06)

主引用文献

Ma, X.,Xu, H.,Tong, Y.,Luo, Y.,Dong, Q.,Jiang, T.
Structural and functional investigations of syn-copalyl diphosphate synthase from Oryza sativa.
Commun Chem, 6:240-240, 2023

PubMed Abstract: The large superfamily of labdane-related diterpenoids is defined by the cyclization of linear geranylgeranyl pyrophosphate (GGPP), catalyzed by copalyl diphosphate synthases (CPSs) to form the basic decalin core, the copalyl diphosphates (CPPs). Three stereochemically distinct CPPs have been found in plants, namely (+)-CPP, ent-CPP and syn-CPP. Here, we used X-ray crystallography and cryo-EM methods to describe different oligomeric structures of a syn-copalyl diphosphate synthase from Oryza sativa (OsCyc1), and provided a cryo-EM structure of OsCyc1 mutant in complex with the substrate GGPP. Further analysis showed that tetramers are the dominant form of OsCyc1 in solution and are not necessary for enzyme activity in vitro. Through rational design, we identified an OsCyc1 mutant that can generate ent-CPP in addition to syn-CPP. Our work provides a structural and mechanistic basis for comparing different CPSs and paves the way for further enzyme design to obtain diterpene derivatives with specific chirality.

PubMed: 37932442
DOI: 10.1038/s42004-023-01042-w

実験手法

ELECTRON MICROSCOPY (3.5 Å)