3WMD

Crystal structure of epoxide hydrolase MonBI

3WMD の概要

• エントリーDOI: 10.2210/pdb3wmd/pdb
• 分子名称: Probable monensin biosynthesis isomerase (2 entities in total)
• 機能のキーワード: ntf2-like, epoxide-opening cyclic ether formation, isomerase
• 由来する生物種: Streptomyces cinnamonensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35616.64

構造登録者

Minami, A.,Ose, T.,Sato, K.,Oikawa, A.,Kuroki, K.,Maenaka, K.,Oguri, H.,Oikawa, H. (登録日: 2013-11-16, 公開日: 2014-01-15, 最終更新日: 2024-03-20)

主引用文献

Minami, A.,Ose, T.,Sato, K.,Oikawa, A.,Kuroki, K.,Maenaka, K.,Oguri, H.,Oikawa, H.
Allosteric regulation of epoxide opening cascades by a pair of epoxide hydrolases in monensin biosynthesis
Acs Chem.Biol., 9:562-569, 2014

PubMed Abstract: Multistep catalysis of epoxide hydrolase/cyclase in the epoxide opening cascade is an intriguing issue in polyether biosynthesis. A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved in monensin biosynthesis, we found that MonBII and catalytically inactive MonBI mutant catalyzed two-step reactions of bisepoxide substrate analogue to afford bicyclic product although MonBII alone catalyzed only the first cyclization. The X-ray crystal structure of MonBI dimers suggested the importance of the KSD motif in MonBI/MonBI interaction, which was further supported by gel filtration chromatography of wild-type MonBI and mutant MonBI. The involvement of the KSD motif in heterodimer formation was confirmed by in vitro assay. Direct evidence of MonBI/MonBII interaction was obtained by native mass spectrometry. Its dissociation constant was determined as 2.21 × 10(-5) M by surface plasmon resonance. Our results suggested the involvement of an allosteric regulation mechanism by MonBI/MonBII interaction in monensin skeletal construction.

PubMed: 24320215
DOI: 10.1021/cb4006485

実験手法

X-RAY DIFFRACTION (1.999 Å)