Characterization of a C-methyltransferase from <i>Streptomyces griseoviridis</i> - crystal structure, mechanism, and substrate scope.

ABSTRACT: Despite the presence of pyrroloindoles in many natural products with diverse biological activities, their synthesis remains challenging in terms of stereoselectivity, especially with respect to methylation at the indole C3 position. In the present study, the pyrroloindole motif in tryptophan-based diketopiperazines (DKPs) is synthesized using the SAM-dependent methyltransferase SgMT from Streptomyces griseoviridis. The three-dimensional structure of this indole C3-methyltransferase was determined by X-ray crystallography, providing insights into the enzyme. The complex active site was explored by site-directed mutagenesis, highlighting an intriguing network of tyrosine side chains that is involved in catalytic activity. The enzyme's precise substrate requirements were characterized

SUBMITTER: Haase M 

PROVIDER: S-EPMC11804793 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature