Dynamics and mechanistic interpretations of nonribosomal peptide synthetase cyclization domains |
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| Affiliation: | 1. Department of Chemistry, University of Massachusetts Boston, Boston, MA, 02125, USA;2. Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA |
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| Abstract: | Ox-/thiazoline groups in nonribosomal peptides are formed by a variant of peptide-forming condensation domains called heterocyclization (Cy) domains and appear in a range of pharmaceutically important natural products and virulence factors. Recent cryo-EM, crystallographic, and NMR studies of Cy domains make it opportune to revisit outstanding questions regarding their molecular mechanisms. This review covers structural and dynamical findings about Cy domains that will inform future bioengineering efforts and our understanding of natural product synthesis. |
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| Keywords: | Heterocycle Pantetheine Cyclodehydration Bioengineering Protein–protein interactions Allostery |
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