8qdh

Engineered LmrR carrying a cyclic boronate ester formed between Tris and p-boronophenylalanine at position 89

spinqualitylabelsall models 8qdh, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qdh 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 1.72Å Ligands: GOL, SD0 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2RI36_LACLM Publication Abstract from PubMed Enzymes play an increasingly important role in improving the benignity and efficiency of chemical production, yet the diversity of their applications lags heavily behind chemical catalysts as a result of the relatively narrow range of reaction mechanisms of enzymes. The creation of enzymes containing non-biological functionalities facilitates reaction mechanisms outside nature's canon and paves the way towards fully programmable biocatalysis(1-3). Here we present a completely genetically encoded boronic-acid-containing designer enzyme with organocatalytic reactivity not achievable with natural or engineered biocatalysts(4,5). This boron enzyme catalyses the kinetic resolution of hydroxyketones by oxime formation, in which crucial interactions with the protein scaffold assist in the catalysis. A directed evolution campaign led to a variant with natural-enzyme-like enantioselectivities for several different substrates. The unique activation mode of the boron enzyme was confirmed using X-ray crystallography, high-resolution mass spectrometry (HRMS) and (11)B NMR spectroscopy. Our study demonstrates that genetic-code expansion can be used to create evolvable enantioselective enzymes that rely on xenobiotic catalytic moieties such as boronic acids and access reaction mechanisms not reachable through catalytic promiscuity of natural or engineered enzymes. Boron catalysis in a designer enzyme.,Longwitz L, Leveson-Gower RB, Rozeboom HJ, Thunnissen AWH, Roelfes G Nature. 2024 May;629(8013):824-829. doi: 10.1038/s41586-024-07391-3. Epub 2024 , May 8. PMID:38720081 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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