Molecular basis for acyl carrier protein-ketoreductase interaction in trans-acyltransferase polyketide synthases.

ABSTRACT: The biosynthesis of polyketides by type I modular polyketide synthases (PKS) relies on co-ordinated interactions between acyl carrier protein (ACP) domains and catalytic domains within the megasynthase. Despite the importance of these interactions, and their implications for biosynthetic engineering efforts, they remain poorly understood. Here, we report the molecular details of the interaction interface between an ACP domain and a ketoreductase (KR) domain from a trans-acyltransferase (trans-AT) PKS. Using a high-throughput mass spectrometry (MS)-based assay in combination with scanning alanine mutagenesis, residues contributing to the KR-binding epitope of the ACP domain were identified. Application of carbene footprinting revealed the ACP-binding site on the KR domain surf

SUBMITTER: Passmore M 

PROVIDER: S-EPMC8549798 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature