The inherent flexibility of type I non-ribosomal peptide synthetase multienzymes drives their catalytic activities.

ABSTRACT: Non-ribosomal peptide synthetases (NRPSs) are multienzymes that produce complex natural metabolites with many applications in medicine and agriculture. They are composed of numerous catalytic domains that elongate and chemically modify amino acid substrates or derivatives and of non-catalytic carrier protein domains that can tether and shuttle the growing products to the different catalytic domains. The intrinsic flexibility of NRPSs permits conformational rearrangements that are required to allow interactions between catalytic and carrier protein domains. Their large size coupled to this flexibility renders these multi-domain proteins very challenging for structural characterization. Here, we summarize recent studies that offer structural views of multi-domain NRPSs in various catalytical

SUBMITTER: Bonhomme S 

PROVIDER: S-EPMC8150014 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature