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Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB

Cited 16 time in Web of Science Cited 15 time in Scopus
Authors

Song, Inseok; Kim, Younghyeon; Yu, Jaeseung; Go, Su Yong; Lee, Hong Geun; Song, Woon Ju; Kim, Seokhee

Issue Date
2021-11
Publisher
Nature Publishing Group
Citation
Nature Chemical Biology, Vol.17 No.11, pp.1123-1131
Abstract
Graspetides, also known as omega-ester-containing peptides (OEPs), are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) bearing side chain-to-side chain macrolactone or macrolactam linkages. Here, we present the molecular details of precursor peptide recognition by the macrocyclase enzyme PsnB in the biosynthesis of plesiocin, a group 2 graspetide. Biochemical analysis revealed that, in contrast to other RiPPs, the core region of the plesiocin precursor peptide noticeably enhanced the enzyme-precursor interaction via the conserved glutamate residues. We obtained four crystal structures of symmetric or asymmetric PsnB dimers, including those with a bound core peptide and a nucleotide, and suggest that the highly conserved Arg213 at the enzyme active site specifically recognizes a ring-forming acidic residue before phosphorylation. Collectively, this study provides insights into the mechanism underlying substrate recognition in graspetide biosynthesis and lays a foundation for engineering new variants. Structural and biochemical analysis of the plesiocin macrocyclase enzyme PsnB revealed that, unlike other ribosomal natural products, the core region of the precursor peptide enhances its interaction with the enzyme via conserved glutamate residues.
ISSN
1552-4450
URI
https://hdl.handle.net/10371/202912
DOI
https://doi.org/10.1038/s41589-021-00855-x
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  • College of Natural Sciences
  • Department of Chemistry
Research Area Biochemistry, Inorganic, 무기화학, 생화학

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