Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase.

ABSTRACT: Non-ribosomal peptide synthetases (NRPS) and polyketide synthases (PKS) produce numerous secondary metabolites with various therapeutic/antibiotic properties. Like fatty acid synthases (FAS), these enzymes are organized in modular assembly lines in which each module, made of conserved domains, incorporates a given monomer unit into the growing chain. Knowledge about domain or module interactions may enable reengineering of this assembly line enzymatic organization and open avenues for the design of new bioactive compounds with improved therapeutic properties. So far, little structural information has been available on how the domains interact and communicate. This may be because of inherent interdomain mobility hindering crystallization, or because crystallized molecules may not represent

SUBMITTER: Frueh DP 

PROVIDER: S-EPMC2597408 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature