4RZM

Crystal structure of the Lsd19-lasalocid A complex

4RZM の概要

• エントリーDOI: 10.2210/pdb4rzm/pdb
• 関連するPDBエントリー: 3RGA
• 分子名称: Epoxide hydrolase LasB, Lasalocid A, GLYCEROL, ... (7 entities in total)
• 機能のキーワード: ntf2-like fold, epoxide-opening cyclic ether formation, isomerization, isomerase
• 由来する生物種: Streptomyces lasaliensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62920.04

構造登録者

Mathews, I.I.,Hotta, K.,Chen, X.,Kim, C.-Y. (登録日: 2014-12-22, 公開日: 2015-01-21, 最終更新日: 2023-09-20)

主引用文献

Wong, F.T.,Hotta, K.,Chen, X.,Fang, M.,Watanabe, K.,Kim, C.Y.
Epoxide hydrolase-lasalocid a structure provides mechanistic insight into polyether natural product biosynthesis.
J.Am.Chem.Soc., 137:86-89, 2015

PubMed Abstract: Biosynthesis of some polyether natural products involves a kinetically disfavored epoxide-opening cyclic ether formation, a reaction termed anti-Baldwin cyclization. One such example is the biosynthesis of lasalocid A, an ionophore antibiotic polyether. During lasalocid A biosynthesis, an epoxide hydrolase, Lsd19, converts the bisepoxy polyketide intermediate into the tetrahydrofuranyl-tetrahydropyran product. We report the crystal structure of Lsd19 in complex with lasalocid A. The structure unambiguously shows that the C-terminal domain of Lsd19 catalyzes the intriguing anti-Baldwin cyclization. We propose a general mechanism for epoxide selection by ionophore polyether epoxide hydrolases.

PubMed: 25535803
DOI: 10.1021/ja511374k

実験手法

X-RAY DIFFRACTION (2.33 Å)