8ZF1
Crystal structure of a Chemo Triplet Photoenzyme (CTPe)
Summary for 8ZF1
| Entry DOI | 10.2210/pdb8zf1/pdb |
| Descriptor | Transcriptional regulator, PadR-like family, N-(9-oxidanylidenethioxanthen-2-yl)ethanamide (2 entities in total) |
| Functional Keywords | aritificial enzyme, protein modification, biocatalysis, energy transfer, photosynthesis |
| Biological source | Lactococcus lactis subsp. cremoris (strain MG1363) |
| Total number of polymer chains | 1 |
| Total formula weight | 15280.23 |
| Authors | Chen, X.,Qian, J.Y.,Guo, J.,Wu, Y.Z.,Zhong, F.R. (deposition date: 2024-05-07, release date: 2024-07-17, Last modification date: 2024-11-13) |
| Primary citation | Guo, J.,Qian, J.,Cai, D.,Huang, J.,Yang, X.,Sun, N.,Zhang, J.,Pang, T.,Zhao, W.,Wu, G.,Chen, X.,Zhong, F.,Wu, Y. Chemogenetic Evolution of Diversified Photoenzymes for Enantioselective [2 + 2] Cycloadditions in Whole Cells. J.Am.Chem.Soc., 146:19030-19041, 2024 Cited by PubMed Abstract: Artificial photoenzymes with novel catalytic modes not found in nature are in high demand; yet, they also present significant challenges in the field of biocatalysis. In this study, a chemogenetic modification strategy is developed to facilitate the rapid diversification of photoenzymes. This strategy integrates site-specific chemical conjugation of various artificial photosensitizers into natural protein cavities and the iterative mutagenesis in cell lysates. Through rounds of directed evolution, prominent visible-light-activatable photoenzyme variants were developed, featuring a thioxanthone chromophore. They successfully enabled the enantioselective [2 + 2] photocycloaddition of 2-carboxamide indoles, a class of UV-sensitive substrates that are traditionally challenging for known photoenzymes. Furthermore, the versatility of this photoenzyme is demonstrated in enantioselective whole-cell photobiocatalysis, enabling the efficient synthesis of enantioenriched cyclobutane-fused indoline tetracycles. These findings significantly expand the photophysical properties of artificial photoenzymes, a critical factor in enhancing their potential for harnessing excited-state reactivity in stereoselective transformations. PubMed: 38976645DOI: 10.1021/jacs.4c03087 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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