6i8n

Crystal structure of LmrR with V15 replaced by unnatural amino acid 4-amino-L-phenylalanine

spinqualitylabelsall models 6i8n, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6i8n is a 2 chain structure with sequence from Lactococcus lactis subsp. cremoris MG1363. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.79Å Ligands: HOX, MPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2RI36_LACLM Publication Abstract from PubMed The impressive rate accelerations that enzymes display in nature often result from boosting the inherent catalytic activities of side chains by their precise positioning inside a protein binding pocket. Here we show that such fine-tuning is also possible for catalytic unnatural amino acids. Specifically, we report the directed evolution of a recently described designer enzyme, which utilizes an aniline side chain to promote a model hydrazone formation reaction. Consecutive rounds of directed evolution identified a number of mutations in the promiscuous binding pocket, in which the unnatural amino acid is embedded in the starting catalyst. When combined, these mutations boost the turnover frequency (kcat) of the designer enzyme by almost 100-fold. Crucially, these gains result from strengthening the catalytic contribution of the unnatural amino acid, as the engineered designer enzymes outperform variants, in which the aniline side chain is replaced with a catalytically inactive tyrosine residue, by >200-fold. Directed evolution of a designer enzyme featuring an unnatural catalytic amino acid.,Mayer C, Dulson C, Reddem E, Thunnissen AM, Roelfes G Angew Chem Int Ed Engl. 2018 Dec 21. doi: 10.1002/anie.201813499. PMID:30575260 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcriptional activator 3D structures

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