8TJK

SAM-dependent methyltransferase RedM bound to SAH

8TJK の概要

• エントリーDOI: 10.2210/pdb8tjk/pdb
• 分子名称: RedM, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: methyltransferase, indolocarbazole, conformational change, biosynthetic protein
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76560.03

構造登録者

Daniel-Ivad, P.,Ryan, K.S. (登録日: 2023-07-22, 公開日: 2023-12-13, 最終更新日: 2024-01-10)

主引用文献

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

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: 38042494
DOI: 10.1016/j.jbc.2023.105520

実験手法

X-RAY DIFFRACTION (1.85 Å)