Summary for 8QCW
| Entry DOI | 10.2210/pdb8qcw/pdb |
| Descriptor | non-specific serine/threonine protein kinase (2 entities in total) |
| Functional Keywords | kinase, gsk3beta-like, transferase |
| Biological source | Lotus japonicus |
| Total number of polymer chains | 1 |
| Total formula weight | 52776.21 |
| Authors | Leonidas, D.D.,Solovou, T. (deposition date: 2023-08-28, release date: 2024-02-21, Last modification date: 2024-10-23) |
| Primary citation | Solovou, T.G.A.,Stravodimos, G.,Papadopoulos, G.E.,Skamnaki, V.T.,Papadopoulou, K.,Leonidas, D.D. Biochemical and Structural Studies of LjSK1, a Lotus japonicus GSK3 beta /SHAGGY-like Kinase, Reveal Its Functional Role. J.Agric.Food Chem., 72:3763-3772, 2024 Cited by PubMed Abstract: The crystal structure of a truncated form of the glycogen synthase kinase 3β (GSK3β) like kinase (LjSK1) has been resolved at 2.9 Å resolution, providing, for the first time, structural data for a plant GKS3β like kinase. The 3D structure of LjSK1 revealed conservation at the structural level for this plant member of the GSK3β family. However, comparative structural analysis to the human homologue revealed significant differences at the N- and C-termini, supporting the notion for an additional regulatory mechanism in plant GSK3-like kinases. Structural similarities at the catalytic site and the ATP binding site explained the similarity in the function of the human and plant protein. LjSK1 and lupeol are strongly linked to symbiotic bacterial infection and nodulation initiation. An inhibitory capacity of lupeol (IC = 0.77 μM) for LjSK1 was discovered, providing a biochemical explanation for the involvement of these two molecules in nodule formation, and constituted LjSK1 as a molecular target for the discovery of small molecule modulators for crop protection and development. Studies on the inhibitory capacity of two phytogenic triterpenoids (betulinic acid and hederacoside C) to LjSK1 provided their structure-activity relationship and showed that hederacoside C can be the starting point for such endeavors. PubMed: 38330914DOI: 10.1021/acs.jafc.3c07101 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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