Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 35, Issue -, Pages 89-96Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2016.09.005
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Funding
- National Institutes of Health [GM116957, AI116998]
- National Science Foundation [1158169]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1158169] Funding Source: National Science Foundation
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Nonribosomal peptide synthetases (NRPSs) catalyze the assembly line biosynthesis of peptide natural products that play important roles in microbial signaling and communication. These multidomain enzymes use an integrated carrier protein that delivers the growing peptide to the catalytic domains, requiring coordinated conformational changes that allow the proper sequence of synthetic steps. Recent structural studies of NRPSs have described important conformational states and illustrate the critical role of a small subdomain within the adenylation domains. This subdomain alternates between catalytic conformations and also serves as a linker domain, providing further conformational flexibility to enable the carrier to project from the core of NRPS. These studies are described along with remaining questions in the study of the structural dynamics of NRPSs.
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