8q5e | pdb_00008q5e

Crystal structure of PpSB1-LOV protein from Pseudomonas putida with covalent FMN

spinqualitylabelsall models 8q5e, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8q5e is a 2 chain structure with sequence from Pseudomonas putida KT2440. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: FMN, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q88E39_PSEPK Publication Abstract from PubMed Most flavin-dependent enzymes contain a dissociable flavin cofactor. We present a new approach for installing in vivo a covalent bond between a flavin cofactor and its host protein. By using a flavin transferase and carving a flavinylation motif in target proteins, we demonstrate that "dissociable" flavoproteins can be turned into covalent flavoproteins. Specifically, four different flavin mononucleotide-containing proteins were engineered to undergo covalent flavinylation: a light-oxygen-voltage domain protein, a mini singlet oxygen generator, a nitroreductase, and an old yellow enzyme-type ene reductase. Optimizing the flavinylation motif and expression conditions led to the covalent flavinylation of all four flavoproteins. The engineered covalent flavoproteins retained function and often exhibited improved performance, such as higher thermostability or catalytic performance. The crystal structures of the designed covalent flavoproteins confirmed the designed threonyl-phosphate linkage. The targeted flavoproteins differ in fold and function, indicating that this method of introducing a covalent flavin-protein bond is a powerful new method to create flavoproteins that cannot lose their cofactor, boosting their performance. Fixing Flavins: Hijacking a Flavin Transferase for Equipping Flavoproteins with a Covalent Flavin Cofactor.,Tong Y, Kaya SG, Russo S, Rozeboom HJ, Wijma HJ, Fraaije MW J Am Chem Soc. 2023 Dec 13;145(49):27140-27148. doi: 10.1021/jacs.3c12009. Epub , 2023 Dec 4. PMID:38048072 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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