9FOA
Artificial photoenzyme with anthraquinone cofactor and wild type streptavidin
This is a non-PDB format compatible entry.
Summary for 9FOA
| Entry DOI | 10.2210/pdb9foa/pdb |
| Related | 9FFJ 9FNR |
| Descriptor | Streptavidin, ~{N}-[4-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]butyl]-9,10-bis(oxidanylidene)anthracene-2-carboxamide, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | artificial photoenzyme, anthraquinone, metal binding protein |
| Biological source | Streptomyces avidinii |
| Total number of polymer chains | 1 |
| Total formula weight | 17298.80 |
| Authors | Lau, K.,Wang, W.,Pojer, F.,Larabi, A. (deposition date: 2024-06-11, release date: 2025-01-15, Last modification date: 2025-02-26) |
| Primary citation | Wang, W.,Tachibana, R.,Zhang, K.,Lau, K.,Pojer, F.,Ward, T.R.,Hu, X. Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations. Angew.Chem.Int.Ed.Engl., 64:e202422783-e202422783, 2025 Cited by PubMed Abstract: Artificial metalloenzymes (ArMs) enable the integration of abiotic cofactors within a native protein scaffold, allowing for non-natural catalytic activities. Previous ArMs, however, have primarily relied on single cofactor systems, limiting them to only one catalytic function. Here we present an approach to construct ArMs embedding two catalytic cofactors based on the biotin-streptavidin technology. By incorporating multiple catalytic cofactors into the four binding sites of streptavidin, we engineered programmable ArMs for tandem abiotic transformations including an enantioselective formal C-H hydroxylation and a photooxidation-Michael addition. This work thus outlines a promising strategy for the development of ArMs embedding multiple cofactors. PubMed: 39760306DOI: 10.1002/anie.202422783 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.36 Å) |
Structure validation
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