4UHB

Laboratory evolved variant R-C1 of potato epoxide hydrolase StEH1

4UHB の概要

• エントリーDOI: 10.2210/pdb4uhb/pdb
• 分子名称: EPOXIDE HYDROLASE, GLYCEROL, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: hydrolase, directed evolution
• 由来する生物種: SOLANUM TUBEROSUM (POTATO)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75296.11

構造登録者

Nilsson, M.T.I.,Carlsson, A.J.,Dobritzsch, D.,Widersten, M. (登録日: 2015-03-23, 公開日: 2016-04-13, 最終更新日: 2024-01-10)

主引用文献

Janfalk Carlsson, A.,Bauer, P.,Dobritzsch, D.,Nilsson, M.,Kamerlin, S.C.,Widersten, M.
Laboratory Evolved Enzymes Provide Snapshots of the Development of Enantioconvergence in Enzyme-Catalyzed Epoxide Hydrolysis.
Chembiochem, 17:1693-, 2016

PubMed Abstract: Engineered enzyme variants of potato epoxide hydrolase (StEH1) display varying degrees of enrichment of (2R)-3-phenylpropane-1,2-diol from racemic benzyloxirane. Curiously, the observed increase in the enantiomeric excess of the (R)-diol is not only a consequence of changes in enantioselectivity for the preferred epoxide enantiomer, but also to changes in the regioselectivity of the epoxide ring opening of (S)-benzyloxirane. In order to probe the structural origin of these differences in substrate selectivity and catalytic regiopreference, we solved the crystal structures for the evolved StEH1 variants. We used these structures as a starting point for molecular docking studies of the epoxide enantiomers into the respective active sites. Interestingly, despite the simplicity of our docking analysis, the apparent preferred binding modes appear to rationalize the experimentally determined regioselectivities. The analysis also identifies an active site residue (F33) as a potentially important interaction partner, a role that could explain the high conservation of this residue during evolution. Overall, our experimental, structural, and computational studies provide snapshots into the evolution of enantioconvergence in StEH1-catalyzed epoxide hydrolysis.

PubMed: 27383542
DOI: 10.1002/CBIC.201600330

実験手法

X-RAY DIFFRACTION (1.8 Å)