8EA2

Structure of 2-hydroxyisoflavanone dehydratase from Pueraria lobate

8EA2 の概要

• エントリーDOI: 10.2210/pdb8ea2/pdb
• 分子名称: 2-hydroxyisoflavanone dehydratase (2 entities in total)
• 機能のキーワード: dehydratase, dehydration, carboxylesterase, plant protein
• 由来する生物種: Pueraria montana var. lobata (kudzu vine)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38919.98

構造登録者

Pan, H.,Wang, X. (登録日: 2022-08-27, 公開日: 2022-11-30, 最終更新日: 2023-10-25)

主引用文献

Wang, X.,Pan, H.,Sagurthi, S.,Paris, V.,Zhuo, C.,Dixon, R.A.
The protein conformational basis of isoflavone biosynthesis.
Commun Biol, 5:1249-1249, 2022

PubMed Abstract: Isoflavonoids play important roles in plant defense and also exhibit a range of mammalian health-promoting activities. Their biosynthesis is initiated by two enzymes with unusual catalytic activities; 2-hydroxyisoflavanone synthase (2-HIS), a membrane-bound cytochrome P450 catalyzing a coupled aryl-ring migration and hydroxylation, and 2-hydroxyisoflavanone dehydratase (2-HID), a member of a large carboxylesterase family that paradoxically catalyzes dehydration of 2-hydroxyisoflavanones to isoflavone. Here we report the crystal structures of 2-HIS from Medicago truncatula and 2-HID from Pueraria lobata. The 2-HIS structure reveals a unique cytochrome P450 conformation and heme and substrate binding mode that facilitate the coupled aryl-ring migration and hydroxylation reactions. The 2-HID structure reveals the active site architecture and putative catalytic residues for the dual dehydratase and carboxylesterase activities. Mutagenesis studies revealed key residues involved in substrate binding and specificity. Understanding the structural basis of isoflavone biosynthesis will facilitate the engineering of new bioactive isoflavonoids.

PubMed: 36376429
DOI: 10.1038/s42003-022-04222-x

実験手法

X-RAY DIFFRACTION (2.394 Å)