7wj7 | pdb_00007wj7

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

spinqualitylabelsall models 7wj7, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7wj7 is a 2 chain structure with sequence from Thermomonospora curvata DSM 43183. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Ligands: XYA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D1ABX1_THECD Publication Abstract from PubMed Class III lanthipeptide synthetases catalyze the formation of lanthionine/methyllanthionine and labionin crosslinks. We present here the 2.40 A 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. Discovery of a Unique Structural Motif in Lanthipeptide Synthetases for Substrate Binding and Interdomain Interactions.,Huang S, Wang Y, Cai C, Xiao X, Liu S, Ma Y, Xie X, Liang Y, Chen H, Zhu J, Hegemann JD, Yao H, Wei W, Wang H Angew Chem Int Ed Engl. 2022 Nov 7;61(45):e202211382. doi:, 10.1002/anie.202211382. Epub 2022 Oct 7. PMID:36102578 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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