Gesellschaft Deutscher Chemiker
Keine Benachrichtigungen
Sie haben noch keine Lesezeichen
Abmelden

Artikel

Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions

Von Wiley-VCH zur Verfügung gestellt

Class III lanthipeptide synthetases catalyze the formation of lanthionine/methyllanthionine and labionin crosslinks. We present here the 2.40 Å 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 insights into the substrate recognition and domain organization in multi-domain lanthipeptide synthetases.

Zum Volltext

Überprüfung Ihres Anmeldestatus ...

Wenn Sie ein registrierter Benutzer sind, zeigen wir in Kürze den vollständigen Artikel.