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| Title | Structural insights into the substrate binding mechanism of the class I dehydratase MadB. |
|---|---|
| Journal, issue, pages | Commun Biol, Vol. 8, Issue 1, Page 1032, Year 2025 |
| Publish date | Jul 9, 2025 |
 Authors | C Vivien Knospe / Julio Ortiz / Jens Reiners / Alexej Kedrov / Christoph G W Gertzen / Sander H J Smits / Lutz Schmitt /  |
| PubMed Abstract | In the battle against antimicrobial resistance, lantibiotics have emerged as promising new sources for antimicrobial drugs. Their exceptional stability is due to characteristic modifications termed ...In the battle against antimicrobial resistance, lantibiotics have emerged as promising new sources for antimicrobial drugs. Their exceptional stability is due to characteristic modifications termed (methyl-)lanthionine rings. Genome mining efforts have identified hundreds of lantibiotics by detecting gene operons, so-called biosynthetic gene clusters (BGC), which encode cysteine-rich peptides (30-50 amino acids in size) and enzymes responsible for dehydration and cyclization, catalyzing the post-translational ring formation. One such identified, class I lantibiotic is maddinglicin from Clostridium maddingley. Here, we present single particle cryo-EM structures of the dehydratase MadB in both, its apo-state and in complex with a leader peptide of maddinglicin, revealing a distinct conformational change upon substrate binding. Small-angle X-ray scattering studies elucidate the substrate binding site for the C-terminal part of maddinglicin. Furthermore, a substrate specificity analysis was performed highlighting a critical stretch of amino acids within the maddinglicin leader sequence that is crucial for binding. Here, we provide molecular insights into the conformational changes, principles of substrate recognition and ligand:protein stoichiometry of a class I lantibiotic dehydratase. |
 External links | Commun Biol / PubMed:40634635 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.7 - 3.13 Å |
| Structure data | EMDB-50910, PDB-9g04: EMDB-50911, PDB-9g05: |
| Source |
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 Keywords | BIOSYNTHETIC PROTEIN / lanthipeptides / dehydratases / cryo-EM structure / class I lantibiotic |
Clostridium maddingley (bacteria)