8I70

Crystal structure of NADP-binding form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus

8I70 の概要

• エントリーDOI: 10.2210/pdb8i70/pdb
• 分子名称: Short-chain dehydrogenase/reductase SDR, GLYCEROL, L(+)-TARTARIC ACID, ... (5 entities in total)
• 機能のキーワード: nad(p)-binding protein, short-chain reductase, oxidoreductase
• 由来する生物種: Chloroflexus aurantiacus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76640.45

構造登録者

Kim, S.,Kim, K.-J. (登録日: 2023-01-30, 公開日: 2023-06-14, 最終更新日: 2024-05-29)

主引用文献

Ahn, J.W.,Kim, S.,Hong, J.,Kim, K.J.
Cryo-EM structure of bifunctional malonyl-CoA reductase from Chloroflexus aurantiacus reveals a dynamic domain movement for high enzymatic activity.
Int.J.Biol.Macromol., 242:124676-124676, 2023

PubMed Abstract: The platform chemical 3-hydroxypropionic acid is used to synthesize various valuable materials, including bioplastics. Bifunctional malonyl-CoA reductase is a key enzyme in 3-hydroxypropionic acid biosynthesis as it catalyzes the two-step reduction of malonyl-CoA to malonate semialdehyde to 3-hydroxypropionic acid. Here, we report the cryo-EM structure of a full-length malonyl-CoA reductase protein from Chloroflexus aurantiacus (CaMCR). The EM model of CaMCR reveals a tandem helix architecture comprising an N-terminal (CaMCR) and a C-terminal (CaMCR) domain. The CaMCR model also revealed that the enzyme undergoes a dynamic domain movement between CaMCR and CaMCR due to the presence of a flexible linker between these two domains. Increasing the flexibility and extension of the linker resulted in a twofold increase in enzyme activity, indicating that for CaMCR, domain movement is crucial for high enzyme activity. We also describe the structural features of CaMCR and CaMCR. This study reveals the protein structures underlying the molecular mechanism of CaMCR and thereby provides valuable information for future enzyme engineering to improve the productivity of 3-hydroxypropionic acid.

PubMed: 37146856
DOI: 10.1016/j.ijbiomac.2023.124676

実験手法

X-RAY DIFFRACTION (1.9 Å)