8TJK
SAM-dependent methyltransferase RedM bound to SAH
Summary for 8TJK
| Entry DOI | 10.2210/pdb8tjk/pdb |
| Descriptor | RedM, SULFATE ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | methyltransferase, indolocarbazole, conformational change, biosynthetic protein |
| Biological source | uncultured bacterium |
| Total number of polymer chains | 2 |
| Total formula weight | 76560.03 |
| Authors | Daniel-Ivad, P.,Ryan, K.S. (deposition date: 2023-07-22, release date: 2023-12-13, Last modification date: 2024-01-10) |
| Primary citation | Daniel-Ivad, P.,Ryan, K.S. Structure of methyltransferase RedM that forms the dimethylpyrrolinium of the bisindole reductasporine. J.Biol.Chem., 300:105520-105520, 2023 Cited by PubMed Abstract: Bisindoles are biologically active natural products that arise from the oxidative dimerization of two molecules of l-tryptophan. In bacterial bisindole pathways, a core set of transformations is followed by the action of diverse tailoring enzymes that catalyze reactions that lead to diverse bisindole products. Among bisindoles, reductasporine is distinct due to its dimethylpyrrolinium structure. Its previously reported biosynthetic gene cluster encodes two unique tailoring enzymes, the imine reductase RedE and the dimethyltransferase RedM, which were shown to produce reductasporine from a common bisindole intermediate in recombinant E. coli. To gain more insight into the unique tailoring enzymes in reductasporine assembly, we reconstituted the biosynthetic pathway to reductasporine in vitro and then solved the 1.7 Å resolution structure of RedM. Our work reveals RedM adopts a variety of conformational changes with distinct open and closed conformations, and site-directed mutagenesis alongside sequence analysis identifies important active site residues. Finally, our work sets the stage for understanding how RedM evolved to react with a pyrrolinium scaffold and may enable the development of new dimethyltransferase catalysts. PubMed: 38042494DOI: 10.1016/j.jbc.2023.105520 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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