title: Exploring the domain structure of modular nonribosomal peptide synthetases.
abstract: Recently, considerable insight has been gained into the modular organization of nonribosomal peptide synthetases (NRPS). The three-dimensional structures of domains associated with substrate adenylation and covalent binding have been solved as well as the structure of a priming enzyme required for the post-translational modification of NRPS. Taken together, these studies will help us to understand the architecture of these mega-enzymes.
authors.affiliation: Biochemie/Fachbereich Chemie, Philipps-Universität, 35032 Marburg, Germany.
authors.forename: T
authors.initials: T
authors.lastname: Weber
authors.forename: M A
authors.initials: MA
authors.lastname: Marahiel
mesh_terms: D008958:Models, Molecular; D010453:Peptide Synthases / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary
chemical_list: D010649:Phenylalanine; D010453:Peptide Synthases; C104385:non-ribosomal peptide synthase