6L8H

Crystal structure of CYP97C1

6L8H の概要

• エントリーDOI: 10.2210/pdb6l8h/pdb
• 分子名称: Carotene epsilon-monooxygenase, chloroplastic, PROTOPORPHYRIN IX CONTAINING FE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: lutein biosynthesis, photosynthesis, monooxygenase, carotenoid, p450, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 216418.69

構造登録者

Niu, G.,Guo, Q.,Liu, L. (登録日: 2019-11-06, 公開日: 2020-06-10, 最終更新日: 2023-11-22)

主引用文献

Niu, G.,Guo, Q.,Wang, J.,Zhao, S.,He, Y.,Liu, L.
Structural basis for plant lutein biosynthesis from alpha-carotene.
Proc.Natl.Acad.Sci.USA, 117:14150-14157, 2020

PubMed Abstract: Two cytochrome P450 enzymes, CYP97A3 and CYP97C1, catalyze hydroxylations of the β- and ε-rings of α-carotene to produce lutein. Chirality is introduced at the C-3 atom of both rings, and the reactions are both pro-3-stereospecific. We determined the crystal structures of CYP97A3 in substrate-free and complex forms with a nonnatural substrate and the structure of CYP97C1 in a detergent-bound form. The structures of CYP97A3 in different states show the substrate channel and the structure of CYP97C1 bound with octylthioglucoside confirms the binding site for the carotenoid substrate. Biochemical assays confirm that the ferredoxin-NADP reductase (FNR)-ferredoxin pair is used as the redox partner. Details of the pro-3 stereospecificity are revealed in the retinal-bound CYP97A3 structure. Further analysis indicates that the CYP97B clan bears similarity to the β-ring-specific CYP97A clan. Overall, our research describes the molecular basis for the last steps of lutein biosynthesis.

PubMed: 32513704
DOI: 10.1073/pnas.2001806117

実験手法

X-RAY DIFFRACTION (2 Å)