Molecular impact of covalent modifications on nonribosomal peptide synthetase carrier protein communication.

ABSTRACT: Nonribosomal peptide synthesis involves the interplay between covalent protein modifications, conformational fluctuations, catalysis, and transient protein-protein interactions. Delineating the mechanisms involved in orchestrating these various processes will deepen our understanding of domain-domain communication in nonribosomal peptide synthetases (NRPSs) and lay the groundwork for the rational reengineering of NRPSs by swapping domains handling different substrates to generate novel natural products. Although many structural and biochemical studies of NRPSs exist, few studies have focused on the energetics and dynamics governing the interactions in these systems. Here, we present detailed binding studies of an adenylation domain and its partner carrier protein in apo-, holo-, and substr

SUBMITTER: Goodrich AC 

PROVIDER: S-EPMC5473208 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature