Related Experiment Video
Updated: Aug 20, 2025

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
Published on: September 28, 2022
Dynamics and mechanistic interpretations of nonribosomal peptide synthetase cyclization domains
Andrew D Gnann1, Kenneth Marincin2, Dominique P Frueh2
1Department of Chemistry, University of Massachusetts Boston, Boston, MA, 02125, USA.
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.
More Related Videos
Related Concept Videos
ATP Synthase: Mechanism
Mechanical Protein Functions
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Ribosomal RNA Synthesis
Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
Directing Proteins to the Rough Endoplasmic Reticulum
Coordination of Gene Expression Processes in Bacteria

