ArticleAngewandte Chemie (International ed. in English)2022
Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.
Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 13 citations in OpenAlex.
- Catalytic architecture and cyclase-mediated dimerization of a newly identified class III-c lanthipeptide synthetase.Protein science : a publication of the Protein Society · 2026Article
- LanthMS: A Computational Tool for the Structure Elucidation of Lanthipeptides from Tandem Mass Spectrometry Data.Protein and peptide letters · 2026Article
- A Unique Class of Cyclases with a Kinase Fold Catalyzes Enethiol-Mediated Macrocyclization of Aminovinyl-Cysteine Motifs in Lanthipeptides.ACS central science · 2025Article
- Mechanistic insights into lanthipeptide modification by a distinct subclass of LanKC enzyme that forms dimers.Nature communications · 2024Article
- Disordered regions in proteusin peptides guide post-translational modification by a flavin-dependent RiPP brominase.Nature communications · 2024Article
- Core-dependent post-translational modifications guide the biosynthesis of a new class of hypermodified peptides.Nature communications · 2023Article
- Structure and Function of a Class III Metal-Independent Lanthipeptide Synthetase.ACS central science · 2023Article
- Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.Angewandte Chemie (International ed. in English) · 2022Article
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Authors and funding
14 authors at 5 institutions in 2 countries.
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Abstract
Class III lanthipeptide synthetases catalyze the formation of lanthionine/methyllanthionine and labionin crosslinks. We present here the 2.40 Å resolution structure of the kinase domain of a class III lanthipeptide synthetase CurKC from the biosynthesis of curvopeptin. A unique structural subunit for leader binding, named leader recognition domain (LRD), was identified. The LRD of CurKC is responsible for the recognition of the leader peptide and for mediating interactions between the lyase and kinase domains. LRDs are highly conserved among the kinase domains of class III and class IV lanthipeptide synthetases. The discovery of LRDs provides insight into the substrate recognition and domain organization in multidomain lanthipeptide synthetases.
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