9sx8 | pdb_00009sx8

Crystal structure of eSNAr1.3 (K39A) in complex with 2,4-dinitrobromobenzene

spinqualitylabelsall models 9sx8, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9sx8 is a 1 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: A1JRE, EDO, PEG, PG4, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Enzymes that catalyze non-natural C-C bond-forming reactions are powerful tools in asymmetric synthesis, yet reprogramming their active sites to invert stereochemical outcome remains challenging. Building on our recently engineered S(N)Arase, S(N)Ar1.3, which performs enantioselective nucleophilic aromatic substitutions with carbon nucleophiles, we now report the evolution of an enantiocomplementary biocatalyst (eS(N)Ar1.3) that displays enhanced activity and expanded substrate scope. Structural and computational analyses uncover both conserved and divergent features between S(N)Ar1.3 and eS(N)Ar1.3. Despite retaining similar electrophile binding poses and a conserved catalytic arginine, the halide-binding pocket of S(N)Ar1.3 has been abandoned in eS(N)Ar1.3. Instead, His23 has emerged as a key motif that works with Arg124 to accurately position the nucleophilic substrate. Calculations reveal that Arg124 also plays a crucial role in facilitating halide release during catalysis. Our study demonstrates how evolution can reshape enzyme mechanisms in unforeseen ways, highlighting the importance of exploring diverse trajectories to access new functions. Directed evolution of an enantiocomplementary S(N)Arase reveals divergent catalytic features.,Lister TM, Roberts GW, Duran C, Casadevall G, Zhao F, Millman AAV, Larrosa I, Osuna S, Green AP Nat Commun. 2026 Aug 21;17(1):10033. doi: 10.1038/s41467-026-76922-5. PMID:42767999 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA