5YPT

Crystal structure of Marchantia paleacea chalone synthase like 1 (CHSL1)

5YPT の概要

• エントリーDOI: 10.2210/pdb5ypt/pdb
• 分子名称: Stilbenecarboxylate synthase 1 (2 entities in total)
• 機能のキーワード: chalcone synthase, pks type iii, chsl1, transferase
• 由来する生物種: Marchantia polymorpha (Liverwort)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 279575.15

構造登録者

Lou, H.X.,Yu, H. (登録日: 2017-11-03, 公開日: 2018-07-04, 最終更新日: 2023-11-22)

主引用文献

Yu, H.N.,Liu, X.Y.,Gao, S.,Sun, B.,Zheng, H.B.,Ji, M.,Cheng, A.X.,Lou, H.X.
Structural and biochemical characterization of the plant type III polyketide synthases of the liverwort Marchantia paleacea.
Plant Physiol. Biochem., 125:95-105, 2018

PubMed Abstract: Chalcone synthases (CHSs) of the type III polyketide synthases (PKSs), catalyze the formation of a tetraketide intermediate from a CoA-tethered starter and malonyl-CoA but use different cyclization mechanisms to produce distinct chemical scaffolds. Herein, we characterized CHS and CHS-like enzymes (designated MpCHS and MpCHSL1, 2 and 3) from Marchantia paleacea and determined the crystal structure of MpCHSL1. MpCHS catalyzed a Claisen condensation to form chalcone, while MpCHSLs catalyzed the formation of lactonized α-pyrones in vitro. Based on the structural, mutational and in vitro biochemical analyses, we established that MpCHSL1 is structurally and functionally closer to prototype CHS than stilbene synthase, and characterized the structural basis for the functional diversity of the type III PKSs. A chalcone-forming mutant of MpCHSL1 was build directed by the structural information. These findings pave the way for future studies to elucidate the functional diversity of type III PKSs in liverwort.

PubMed: 29428820
DOI: 10.1016/j.plaphy.2018.01.030

実験手法

X-RAY DIFFRACTION (2.394 Å)