9FYU

Crystal structure of the engineered photoenzyme VEnT1.0

これはPDB形式変換不可エントリーです。

9FYU の概要

• エントリーDOI: 10.2210/pdb9fyu/pdb
• 関連するPDBエントリー: 9FYV
• 分子名称: Diisopropyl-fluorophosphatase, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: photoenzyme, designed enzyme, directed evolution, cycloaddition, genetic code expansion, noncanonical amino acid, biosynthetic protein
• 由来する生物種: Loligo vulgaris
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73028.98

構造登録者

Hardy, F.J.,Roberts, G.W. (登録日: 2024-07-04, 公開日: 2025-05-14, 最終更新日: 2025-07-16)

主引用文献

Crawshaw, R.,Smithson, R.,Hofer, J.,Hardy, F.J.,Roberts, G.W.,Trimble, J.S.,Kohn, A.R.,Levy, C.W.,Drost, D.A.,Merten, C.,Heyes, D.J.,Obexer, R.,Bach, T.,Green, A.P.
Efficient and selective energy transfer photoenzymes powered by visible light.
Nat.Chem., 17:1083-1090, 2025

PubMed Abstract: The development of [2 + 2] cyclases containing benzophenone triplet sensitizers highlights the potential of engineered enzymes as a platform for stereocontrolled energy transfer photocatalysis. However, the suboptimal photophysical features of benzophenone necessitates the use of ultraviolet light, limits photochemical efficiency and restricts the range of chemistries accessible. Here we engineer an orthogonal Methanococcus jannaschii tyrosyl-tRNA synthetase/tRNA pair for encoding thioxanthone triplet sensitizers into proteins, which can efficiently harness visible light to drive photochemical conversions. Initially, we developed an enantioselective [2 + 2] cyclase that is orders of magnitude more efficient than our previously developed photoenzymes (k = 13 s, >1,300 turnovers). To demonstrate that thioxanthone-containing enzymes can enable more challenging photochemical conversions, we developed a second oxygen-tolerant enzyme that can steer selective C-H insertions of excited quinolone substrates to afford spirocyclic β-lactams with high selectivity (99% e.e., 22:1 d.r.). This photoenzyme also suppresses a competing substrate decomposition pathway observed with small-molecule sensitizers, underscoring the ability of engineered enzymes to control the fate of excited-state intermediates.

PubMed: 40329013
DOI: 10.1038/s41557-025-01820-0

実験手法

X-RAY DIFFRACTION (1.52 Å)