7WJ7

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

7WJ7 の概要

• エントリーDOI: 10.2210/pdb7wj7/pdb
• 分子名称: Serine/threonine protein kinase, 2-(6-AMINO-OCTAHYDRO-PURIN-9-YL)-5-HYDROXYMETHYL-TETRAHYDRO-FURAN-3,4-DIOL (3 entities in total)
• 機能のキーワード: lanthipeptide synthetase, class iii, curkc, curvopeptin, biosynthetic protein
• 由来する生物種: Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60891.09

構造登録者

Huang, S.,Wang, H. (登録日: 2022-01-05, 公開日: 2022-11-09, 最終更新日: 2023-11-29)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.55 Å)