9gkt | pdb_00009gkt

Crystal structure of artificial enzyme LmrR_pAF variant RGN

spinqualitylabelsall models 9gkt, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9gkt 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 2.45Å Ligands: HOX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A2RI36_LACLM Publication Abstract from PubMed The evolution of a promiscuous enzyme for its various activities often results in catalytically specialized variants. This is an important natural mechanism to ensure the proper functioning of natural metabolic networks. It also acts as both a curse and blessing for enzyme engineers, where enzymes that have undergone directed evolution may exhibit exquisite selectivity at the expense of a diminished overall catalytic repertoire. We previously performed two independent directed evolution campaigns on a promiscuous designer enzyme that leverages the unique properties of a noncanonical amino acid (ncAA) para-aminophenylalanine (pAF) as catalytic residue, resulting in two evolved variants which are both catalytically specialized. Here, we combine mutagenesis, crystallography, and computation to reveal the molecular basis of the specialization phenomenon. In one evolved variant, an unexpected change in quaternary structure biases substrate dynamics to promote enantioselective catalysis, while the other demonstrates synergistic cooperation between natural side chains and the pAF residue to form semisynthetic catalytic machinery. Evolutionary Specialization of a Promiscuous Designer Enzyme.,Leveson-Gower RB, Tiessler-Sala L, Rozeboom HJ, Thunnissen AWH, Marechal JD, Roelfes G ACS Catal. 2025 Jan 13;15(3):1544-1552. doi: 10.1021/acscatal.4c06409. , eCollection 2025 Feb 7. PMID:39944761 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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