Abstract
This viewpoint article focuses on the structures of the dissected catalytic domains of non-ribosomal peptide synthetases (NRPSs) associated with substrate selection and activation (A domain), substrate shuttling among the active sites (PCP domain), peptide bond formation (C domain) and product release (TE domain). Structural details of these essential components of the NRPS machinery, integrated in a didomain (PCP-C) and an elongation module (C-A-PCP), were used to generate a model for a multimodular NRPS assembly line.
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