ArticleNature chemical biology2021
Molecular mechanism underlying substrate recognition of the peptide macrocyclase PsnB.
Article in Nature chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 25 citations in OpenAlex.
- Discovery of Partner Protein-Dependent Graspetide Biosynthesis.ACS chemical biology · 2026Article
- Substrate prediction for RiPP biosynthetic enzymesDigital discovery · 2025Article
- α-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.Protein science : a publication of the Protein Society · 2025Article
- Characterization of a Dual Function Peptide Cyclase in Graspetide Biosynthesis.ACS chemical biology · 2024Article
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- Substrate Prediction for RiPP Biosynthetic Enzymes via Masked Language Modeling and Transfer Learning.ArXiv · 2024Article
- Discovery and engineering of ribosomally synthesized and post-translationally modified peptide (RiPP) natural products.RSC chemical biology · 2024Review
- Evolutionary Spread of Distinct O-methyltransferases Guides the Discovery of Unique Isoaspartate-Containing Peptides, Pamtides.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- AlphaFold Accurately Predicts the Structure of Ribosomally Synthesized and Post-Translationally Modified Peptide Biosynthetic Enzymes.Biomolecules · 2023Article
- Discovery, Function, and Engineering of Graspetides.Trends in chemistry · 2023Article
- Emulating nonribosomal peptides with ribosomal biosynthetic strategies.RSC chemical biology · 2023Review
- Article
- Applying Promiscuous RiPP Enzymes to Peptide BackboneACS chemical biology · 2022Article
- Accurate Models of Substrate Preferences of Post-Translational Modification Enzymes from a Combination of mRNA Display and Deep Learning.ACS central science · 2022Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Graspetides, also known as ω-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.
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