9G65
Crystal structure of the engineered photoenzyme SpEnT1.3
This is a non-PDB format compatible entry.
Summary for 9G65
| Entry DOI | 10.2210/pdb9g65/pdb |
| Descriptor | Engineered photoenzyme SpEnT1.3, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (5 entities in total) |
| Functional Keywords | photoenzyme, designed enzyme, directed evolution, cycloaddition, noncanoncial amino acid, biosynthetic protein |
| Biological source | Loligo vulgaris |
| Total number of polymer chains | 1 |
| Total formula weight | 36528.22 |
| Authors | |
| Primary citation | 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., 2025 Cited by 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: 40329013DOI: 10.1038/s41557-025-01820-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
