7XUP

Crystal structure of TPe3.0

7XUP の概要

• エントリーDOI: 10.2210/pdb7xup/pdb
• 分子名称: Transcriptional regulator, PadR-like family (2 entities in total)
• 機能のキーワード: triplet photoenzyme, photocatalysis, energy transfer, photocycloaddition, unnatural amino acid, photosynthesis
• 由来する生物種: Lactococcus lactis subsp. cremoris MG1363
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15135.00

構造登録者

Chen, X.,Qian, J.Y.,Sun, N.N.,Zhong, F.R.,Wu, Y.Z. (登録日: 2022-05-19, 公開日: 2022-09-28, 最終更新日: 2024-05-08)

主引用文献

Sun, N.,Huang, J.,Qian, J.,Zhou, T.P.,Guo, J.,Tang, L.,Zhang, W.,Deng, Y.,Zhao, W.,Wu, G.,Liao, R.Z.,Chen, X.,Zhong, F.,Wu, Y.
Enantioselective [2+2]-cycloadditions with triplet photoenzymes.
Nature, 611:715-720, 2022

PubMed Abstract: Naturally evolved enzymes, despite their astonishingly large variety and functional diversity, operate predominantly through thermochemical activation. Integrating prominent photocatalysis modes into proteins, such as triplet energy transfer, could create artificial photoenzymes that expand the scope of natural biocatalysis. Here, we exploit genetically reprogrammed, chemically evolved photoenzymes embedded with a synthetic triplet photosensitizer that are capable of excited-state enantio-induction. Structural optimization through four rounds of directed evolution afforded proficient variants for the enantioselective intramolecular [2+2]-photocycloaddition of indole derivatives with good substrate generality and excellent enantioselectivities (up to 99% enantiomeric excess). A crystal structure of the photoenzyme-substrate complex elucidated the non-covalent interactions that mediate the reaction stereochemistry. This study expands the energy transfer reactivity of artificial triplet photoenzymes in a supramolecular protein cavity and unlocks an integrated approach to valuable enantioselective photochemical synthesis that is not accessible with either the synthetic or the biological world alone.

PubMed: 36130726
DOI: 10.1038/s41586-022-05342-4

実験手法

X-RAY DIFFRACTION (2.602 Å)