A Topologically Distinct Modified Peptide with Multiple Bicyclic Core Motifs Expands the Diversity of Microviridin‐Like Peptides
| Autor: | Seokhee Kim, Heejin Roh, Yeji Han, Hyunbin Lee |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
Bicyclic molecule 010405 organic chemistry Stereochemistry Organic Chemistry Esters Peptide 010402 general chemistry Ring (chemistry) Peptides Cyclic 01 natural sciences Biochemistry 0104 chemical sciences chemistry Core (graph theory) Side chain Consensus sequence Molecular Medicine Amino Acid Sequence Protein Processing Post-Translational Molecular Biology |
| Zdroj: | ChemBioChem. 20:1051-1059 |
| ISSN: | 1439-7633 1439-4227 |
| Popis: | Microviridins are ribosomally synthesized and post-translationally modified peptides (RiPPs) that contain multiple intramolecular ω-ester or ω-amide crosslinks between two side chains in peptides. This type of the side-to-side macrocyclization may generate diverse structures with distinct topology and ring sizes, but the majority of the microviridin-like RiPPs present only a single consensus sequence with a tricyclic architecture. Here, we expanded the natural diversity of the microviridin-like modified peptides by determining the crosslinking connectivity of a new modified peptide, mTgnA and its homologous RiPPs, which we named the thuringinin group. Members of the thuringinin group have core motifs with a distinct consensus sequence, which is transformed to a novel hairpin-like bicyclic structure by the cognate ATP-grasp enzyme. We suggest that the microviridin-like RiPPs naturally have novel sequences and architectures beyond those found in microviridins and comprise a larger RiPP family, termed omega-ester containing peptides (OEPs). |
| Databáze: | OpenAIRE |
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