9foa

Artificial photoenzyme with anthraquinone cofactor and wild type streptavidin

spinqualitylabelsall models 9foa, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9foa is a 1 chain structure with sequence from Streptomyces avidinii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.36Å Ligands: A1ID2, GOL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SAV_STRAV The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Publication Abstract from PubMed 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. Artificial Metalloenzymes with Two Catalytic Cofactors for Tandem Abiotic Transformations.,Wang W, Tachibana R, Zhang K, Lau K, Pojer F, Ward TR, Hu X Angew Chem Int Ed Engl. 2025 Jan 6:e202422783. doi: 10.1002/anie.202422783. PMID:39760306 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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