7WJ6

Crystal Structure of the Kinase Domain of a Class III Lanthipeptide Synthetase CurKC

Summary for 7WJ6

• Entry DOI: 10.2210/pdb7wj6/pdb
• Descriptor: Serine/threonine protein kinase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: lanthipeptide synthetase, class iii, curkc, curvopeptin, biosynthetic protein
• Biological source: Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9)
• Total number of polymer chains: 2
• Total formula weight: 60502.44

Authors

Huang, S.,Wang, H. (deposition date: 2022-01-05, release date: 2022-11-09, Last modification date: 2023-11-29)

Primary citation

Huang, S.,Wang, Y.,Cai, C.,Xiao, X.,Liu, S.,Ma, Y.,Xie, X.,Liang, Y.,Chen, H.,Zhu, J.,Hegemann, J.D.,Yao, H.,Wei, W.,Wang, H.
Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.
Angew.Chem.Int.Ed.Engl., 61:e202211382-e202211382, 2022

PubMed Abstract: 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.

PubMed: 36102578
DOI: 10.1002/anie.202211382

Experimental method

X-RAY DIFFRACTION (2.55 Å)