Structures of two distinct conformations of holo-non-ribosomal peptide synthetases.

ABSTRACT: Many important natural products are produced by multidomain non-ribosomal peptide synthetases (NRPSs). During synthesis, intermediates are covalently bound to integrated carrier domains and transported to neighbouring catalytic domains in an assembly line fashion. Understanding the structural basis for catalysis with non-ribosomal peptide synthetases will facilitate bioengineering to create novel products. Here we describe the structures of two different holo-non-ribosomal peptide synthetase modules, each revealing a distinct step in the catalytic cycle. One structure depicts the carrier domain cofactor bound to the peptide bond-forming condensation domain, whereas a second structure captures the installation of the amino acid onto the cofactor within the adenylation domain. These structur

SUBMITTER: Drake EJ 

PROVIDER: S-EPMC4843164 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature