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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 Å resolution structure of the kinase domain of a class III lanthipeptide synthetase CurKC from the biosynthesis of curvopeptin. A unique structural subunit fo...

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Detalles Bibliográficos
Autores principales: Huang, Shanqing, Wang, Ying, Cai, Chuangxu, Xiao, Xiuyun, Liu, Shulei, Ma, Yeying, Xie, Xiangqian, Liang, Yong, Chen, Hao, Zhu, Jiapeng, Hegemann, Julian D., Yao, Hongwei, Wei, Wanqing, Wang, Huan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9828337/
https://www.ncbi.nlm.nih.gov/pubmed/36102578
http://dx.doi.org/10.1002/anie.202211382
Descripción
Sumario: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 insight into the substrate recognition and domain organization in multidomain lanthipeptide synthetases.