7XUP
Crystal structure of TPe3.0
Summary for 7XUP
| Entry DOI | 10.2210/pdb7xup/pdb |
| Descriptor | Transcriptional regulator, PadR-like family (2 entities in total) |
| Functional Keywords | triplet photoenzyme, photocatalysis, energy transfer, photocycloaddition, unnatural amino acid, photosynthesis |
| Biological source | Lactococcus lactis subsp. cremoris MG1363 |
| Total number of polymer chains | 1 |
| Total formula weight | 15135.00 |
| Authors | Chen, X.,Qian, J.Y.,Sun, N.N.,Zhong, F.R.,Wu, Y.Z. (deposition date: 2022-05-19, release date: 2022-09-28, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 36130726DOI: 10.1038/s41586-022-05342-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.602 Å) |
Structure validation
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