8rpr | pdb_00008rpr

Crystal Structure of SgvM methyltransferase in complex with alpha-ketoleucine and Zn2+ ion

spinqualitylabelsall models 8rpr, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8rpr is a 1 chain structure with sequence from Streptomyces griseoviridis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.14Å Ligands: CL, COI, MG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function R9UTR3_STRGD Publication Abstract from PubMed S‑adenosyl-l-methionine-dependent methyltransferases (MTs) are involved in the C-methylation of a variety of natural products. The MTs SgvM from Streptomyces griseoviridis and MrsA from Pseudomonas syringae pv. syringae catalyze the methylation of the beta-carbon atom of alpha-keto acids in the biosynthesis of the antibiotic natural products viridogrisein and 3‑methylarginine, respectively. MrsA shows high substrate selectivity for 5‑guanidino-2-oxovalerate, while other alpha-keto acids, such as the SgvM substrates 4-methyl-2-oxovalerate, 2-oxovalerate, and phenylpyruvate, are not accepted. Here we report the crystal structures of SgvM and MrsA in the apo form bound with substrate or S‑adenosyl-l-methionine. By investigating key residues for substrate recognition in the active sites of both enzymes and engineering MrsA by site-directed mutagenesis, the substrate range of MrsA was extended to accept alpha‑keto acid substrates of SgvM with uncharged and lipophilic beta‑residues. Our results showcase the transfer of the substrate scope of alpha-keto acid MTs from different biosynthetic pathways by rational design. Structures and protein engineering of the alpha-keto acid C-methyltransferases SgvM and MrsA for rational substrate transfer.,Sommer-Kamann C, Breiltgens J, Zou Z, Gerhardt S, Saleem-Batcha R, Kemper F, Einsle O, Andexer JN, Muller M Chembiochem. 2024 Jun 18:e202400258. doi: 10.1002/cbic.202400258. PMID:38887142 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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