- PDB-8i6z: Crystal structure of apo-form of malonyl-CoA reductase C-domain f... -
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基本情報
登録情報
データベース: PDB / ID: 8i6z
タイトル
Crystal structure of apo-form of malonyl-CoA reductase C-domain from Chloroflexus aurantiacus
要素
Short-chain dehydrogenase/reductase SDR
キーワード
OXIDOREDUCTASE / NAD(P)-binding protein / Short-chain reductase
機能・相同性
fatty acid elongation / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / short chain dehydrogenase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding domain superfamily / nucleotide binding / metal ion binding / L(+)-TARTARIC ACID / Short-chain dehydrogenase/reductase SDR
ジャーナル: Int J Biol Macromol / 年: 2023 タイトル: Cryo-EM structure of bifunctional malonyl-CoA reductase from Chloroflexus aurantiacus reveals a dynamic domain movement for high enzymatic activity. 著者: Jae-Woo Ahn / Sangwoo Kim / Jiyeon Hong / Kyung-Jin Kim / 要旨: 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 ...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.
履歴
登録
2023年1月30日
登録サイト: PDBJ / 処理サイト: PDBJ
改定 1.0
2023年6月14日
Provider: repository / タイプ: Initial release
改定 1.1
2024年5月29日
Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond
構造決定の手法: 単波長異常分散 / 解像度: 1.95→26.67 Å / Cor.coef. Fo:Fc: 0.969 / Cor.coef. Fo:Fc free: 0.955 / SU B: 2.723 / SU ML: 0.077 / 交差検証法: THROUGHOUT / ESU R: 0.119 / ESU R Free: 0.114 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD / 詳細: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
反射数
%反射
Selection details
Rfree
0.1881
3234
5.2 %
RANDOM
Rwork
0.15643
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obs
0.15806
59137
99.37 %
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溶媒の処理
イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.2 Å / 溶媒モデル: MASK