Journal
CHEMBIOCHEM
Volume 20, Issue 8, Pages 1051-1059Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201800678
Keywords
ATP-grasp; macrocycles; microviridin; peptides; RiPPs
Funding
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Education [2018R1D1A1B07047615]
- Promising-Pioneering Researcher Program through Seoul National University (SNU)
- National Research Foundation of Korea [2018R1D1A1B07047615] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Ask authors/readers for more resources
Microviridins are ribosomally synthesized and post-translationally modified peptides (RiPPs) that contain multiple intramolecular -ester or -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).
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available