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000638191 1001_ $$aKnospe, C. Vivien$$b0
000638191 245__ $$aStructural insights into the substrate binding mechanism of the class I dehydratase MadB
000638191 260__ $$aLondon$$bSpringer Nature$$c2025
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000638191 520__ $$aIn the battle against antimicrobial resistance, lantibiotics have emerged as promising new sources for antimicrobial drugs. Their exceptional stability is due to characteristic modifications termed (methyl-)lanthionine rings. Genome mining efforts have identified hundreds of lantibiotics by detecting gene operons, so-called biosynthetic gene clusters (BGC), which encode cysteine-rich peptides (30-50 amino acids in size) and enzymes responsible for dehydration and cyclization, catalyzing the post-translational ring formation. One such identified, class I lantibiotic is maddinglicin from Clostridium maddingley. Here, we present single particle cryo-EM structures of the dehydratase MadB in both, its apo-state and in complex with a leader peptide of maddinglicin, revealing a distinct conformational change upon substrate binding. Small-angle X-ray scattering studies elucidate the substrate binding site for the C-terminal part of maddinglicin. Furthermore, a substrate specificity analysis was performed highlighting a critical stretch of amino acids within the maddinglicin leader sequence that is crucial for binding. Here, we provide molecular insights into the conformational changes, principles of substrate recognition and ligand:protein stoichiometry of a class I lantibiotic dehydratase.
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000638191 7001_ $$aOrtiz, Julio$$b1
000638191 7001_ $$0P:(DE-HGF)0$$aReiners, Jens$$b2
000638191 7001_ $$00000-0001-9117-752X$$aKedrov, Alexej$$b3
000638191 7001_ $$00000-0002-9562-7708$$aGertzen, Christoph G. W.$$b4
000638191 7001_ $$0P:(DE-HGF)0$$aSmits, Sander H. J.$$b5
000638191 7001_ $$00000-0002-1167-9819$$aSchmitt, Lutz$$b6$$eCorresponding author
000638191 773__ $$0PERI:(DE-600)2919698-X$$a10.1038/s42003-025-08454-5$$gVol. 8, no. 1, p. 1032$$n1$$p1032$$tCommunications biology$$v8$$x2399-3642$$y2025
000638191 8564_ $$uhttps://www.nature.com/articles/s42003-025-08454-5
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