1 research outputs found
Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions
Class III lanthipeptide synthetases catalyze the
formation of lanthionine/methyllanthionine and labionin
crosslinks. We present here the 2.40 Ă… resolution
structure of the kinase domain of a class III lanthipeptide synthetase CurKC from the biosynthesis of curvopeptin. A unique structural subunit for leader binding,
named leader recognition domain (LRD), was identified. The LRD of CurKC is responsible for the
recognition of the leader peptide and for mediating
interactions between the lyase and kinase domains.
LRDs are highly conserved among the kinase domains
of class III and class IV lanthipeptide synthetases. The
discovery of LRDs provides insight into the substrate
recognition and domain organization in multidomain
lanthipeptide synthetases