Stoichiometry and structure of a lantibiotic maturation complex.
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.
Institute of Biochemistry, Heinrich-Heine-University Duesseldorf, Universitaetsstraße 1, 40225 Duesseldorf, Germany.
Jens
J
Reiners
Institute of Biochemistry, Heinrich-Heine-University Duesseldorf, Universitaetsstraße 1, 40225 Duesseldorf, Germany.
André
A
Abts
Institute of Biochemistry, Heinrich-Heine-University Duesseldorf, Universitaetsstraße 1, 40225 Duesseldorf, Germany.
Rebecca
R
Clemens
Institute of Biochemistry, Heinrich-Heine-University Duesseldorf, Universitaetsstraße 1, 40225 Duesseldorf, Germany.
Sander H J
SH
Smits
Institute of Biochemistry, Heinrich-Heine-University Duesseldorf, Universitaetsstraße 1, 40225 Duesseldorf, Germany.
Lutz
L
Schmitt
D000900:Anti-Bacterial Agents / Q000096:biosynthesis / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D005822:Genetic Vectors / Q000737:chemistry / Q000378:metabolism; D019753:Intramolecular Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013294:Lactococcus lactis / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009561:Nisin / Q000096:biosynthesis / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000378:metabolism; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012694:Serine / Q000737:chemistry / Q000378:metabolism; D040681:Structural Homology, Protein; D013379:Substrate Specificity; D013912:Threonine / Q000737:chemistry / Q000378:metabolism
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C079126:NisB protein, Lactococcus lactis; D010455:Peptides; D011994:Recombinant Proteins; D009561:Nisin; D013912:Threonine; D012694:Serine; D019753:Intramolecular Lyases; C522741:NisC protein, E coli