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024 7 _ |a 10.1038/s42003-025-08454-5
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100 1 _ |a Knospe, C. Vivien
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245 _ _ |a Structural insights into the substrate binding mechanism of the class I dehydratase MadB
260 _ _ |a London
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520 _ _ |a 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.
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700 1 _ |a Ortiz, Julio
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700 1 _ |a Reiners, Jens
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700 1 _ |a Kedrov, Alexej
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700 1 _ |a Gertzen, Christoph G. W.
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700 1 _ |a Smits, Sander H. J.
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700 1 _ |a Schmitt, Lutz
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773 _ _ |a 10.1038/s42003-025-08454-5
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856 4 _ |u https://www.nature.com/articles/s42003-025-08454-5
856 4 _ |u https://bib-pubdb1.desy.de/record/638191/files/Structural%20insights%20into%20the%20substrate%20binding%20mechanism%20of%20the%20class%20I%20dehydratase%20MadB.pdf
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