Analysis of the linker region joining the adenylation and carrier protein domains of the modular nonribosomal peptide synthetases.

ABSTRACT: Nonribosomal peptide synthetases (NRPSs) are multimodular proteins capable of producing important peptide natural products. Using an assembly line process, the amino acid substrate and peptide intermediates are passed between the active sites of different catalytic domains of the NRPS while bound covalently to a peptidyl carrier protein (PCP) domain. Examination of the linker sequences that join the NRPS adenylation and PCP domains identified several conserved proline residues that are not found in standalone adenylation domains. We examined the roles of these proline residues and neighboring conserved sequences through mutagenesis and biochemical analysis of the reaction catalyzed by the adenylation domain and the fully reconstituted NRPS pathway. In particular, we identified a conserved

SUBMITTER: Miller BR 

PROVIDER: S-EPMC4177296 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature