ArticleScientific reports2017
Stoichiometry and structure of a lantibiotic maturation complex.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Structural insights into the substrate binding mechanism of the class I dehydratase MadB.Communications biology · 2025Article
- Enabling Access to Novel Bacterial Biosynthetic Potential From ONT Draft Genomic Data.Microbial biotechnology · 2025Article
- After a century of nisin research - where are we now?FEMS microbiology reviews · 2023Review
- Analysis of Cross-Functionality within LanBTC Synthetase Complexes from Different Bacterial Sources with Respect to Production of Fully Modified Lanthipeptides.Applied and environmental microbiology · 2022Article
- The structure of MadC fromFrontiers in microbiology · 2022Article
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- Structural Analysis of Class I Lanthipeptides fromACS chemical biology · 2021Article
- New developments in RiPP discovery, enzymology and engineering.Natural product reports · 2021Review
- Article
- Impact of the nisin modification machinery on the transport kinetics of NisT.Scientific reports · 2020Article
- A Structural View on the Maturation of Lanthipeptides.Frontiers in microbiology · 2020Review
- Characterization of glutamyl-tRNA-dependent dehydratases using nonreactive substrate mimics.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lantibiotics are ribosomally synthesized antimicrobial peptides secreted by mainly Gram-positive bacteria. Class 1 lantibiotics mature via two modification steps introduced by a modification LanBC complex. For the lantibiotic nisin, the dehydratase NisB catalyzes the dehydration of serine and threonine residues in the so-called core peptide. Second, five (methyl)-lanthionine rings are introduced in a regio- and stereospecific manner by the cyclase NisC. Here, we characterized the assembly of the NisBC complex in vitro, which is only formed in the presence of the substrate. The complex is composed of a NisB dimer, a monomer of NisC and one prenisin molecule. Interestingly, the presence of the last lanthionine ring prevented complex formation. This stoichiometry was verified by small-angle X-ray scattering measurements, which revealed the first structural glimpse of a LanBC complex in solution.
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