ArticleJournal of the American Chemical Society2016
Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Biosynthesis, Structure, and Antibiotic Properties of Gelatinamin A, a Triculamin-Like Lasso Peptide.Chembiochem : a European journal of chemical biology · 2026Article
- Discovery and Heterologous Expression of the Soil Metagenome-Derived Lasso Peptide Metanodin with an Unprecedented Ring Structure.Journal of natural products · 2025Article
- Evolution-Guided Discovery of Antimycobacterial Triculamin-Like Lasso Peptides.Angewandte Chemie (International ed. in English) · 2025Article
- Advances in lasso peptide discovery, biosynthesis, and function.Trends in genetics : TIG · 2024Review
- Utilization of lasso peptides for biodegradation of polycyclic aromatic hydrocarbons.Environmental microbiology reports · 2024Article
- Unusual Post-Translational Modifications in the Biosynthesis of Lasso Peptides.International journal of molecular sciences · 2022Review
- Comprehensive Mutational Analysis of the Lasso Peptide Klebsidin.ACS chemical biology · 2022Article
- Rational generation of lasso peptides based on biosynthetic gene mutations and site-selective chemical modifications.Chemical science · 2021Article
- Is the use of recombinant cGnRH may be a future alternative to control the fish spawning? Let us go with the goldfish example.Fish physiology and biochemistry · 2021Article
- Recent Advances and Perspectives on Expanding the Chemical Diversity of Lasso Peptides.Frontiers in bioengineering and biotechnology · 2021Review
- Cutting the Gordian knot: early and complete amino acid sequence confirmation of class II lasso peptides by HCD fragmentation.The Journal of antibiotics · 2020Article
- How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020Review
- Lasso Peptides: Heterologous Production and Potential Medical Application.Frontiers in bioengineering and biotechnology · 2020Review
- Genome mining for lasso peptides: past, present, and future.Journal of industrial microbiology & biotechnology · 2019Review
- Heterologous and in Vitro Reconstitution of Fuscanodin, a Lasso Peptide from Thermobifida fusca.Journal of the American Chemical Society · 2019Article
- Uncovering complex microbiome activities via metatranscriptomics during 24 hours of oral biofilm assembly and maturation.Microbiome · 2018Article
- Cyclic and Lasso Peptides: Sequence Determination, Topology Analysis, and Rotaxane Formation.Angewandte Chemie (International ed. in English) · 2018Article
- Heterologous Production of Microbial Ribosomally Synthesized and Post-translationally Modified Peptides.Frontiers in microbiology · 2018Review
- Genomic Enzymology: Web Tools for Leveraging Protein Family Sequence-Function Space and Genome Context to Discover Novel Functions.Biochemistry · 2017Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Lasso peptides are a class of bioactive ribosomally synthesized and post-translationally modified peptides (RiPPs), with a threaded knot structure that is formed by an isopeptide bond attaching the N-terminus of the peptide to a side chain carboxylate. Some lasso peptide biosynthetic clusters harbor an enzyme that specifically hydrolyzes the isopeptide bond to yield the linear peptide. We describe here the 2.4 Å resolution structure of a lasso peptide isopeptidase revealing a topologically novel didomain architecture consisting of an open β-propeller appended to an α/β hydrolase domain. The 2.2 Å resolution cocrystal structure of an inactive variant in complex with a lasso peptide reveals deformation of the substrate, and reorganization of the enzyme active site, which exposes and orients the isopeptide bond for hydrolysis. Structure-based mutational analysis reveals how this enzyme recognizes the lasso peptide substrate by shape complementarity rather than through sequence specificity. The isopeptidase gene can be used to facilitate genome mining, as a network-based mining strategy queried with this sequence identified 87 putative lasso peptide biosynthetic clusters, 65 of which have not been previously described. Lastly, we validate this mining approach by heterologous expression of two clusters encoded within the genome of Asticcaucalis benevestitus, and demonstrate that both clusters produce lasso peptides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.