6XX9
Arabidopsis thaliana Casein Kinase 2 (CK2) alpha-1 crystal form III
Summary for 6XX9
| Entry DOI | 10.2210/pdb6xx9/pdb |
| Descriptor | Casein kinase II subunit alpha-1, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | kinase, ck2, casein kinase, cell cycle |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 40835.78 |
| Authors | Demulder, M.,De Veylder, L.,Loris, R. (deposition date: 2020-01-27, release date: 2020-04-15, Last modification date: 2024-01-24) |
| Primary citation | Demulder, M.,De Veylder, L.,Loris, R. Crystal structure of Arabidopsis thaliana casein kinase 2 alpha 1. Acta Crystallogr.,Sect.F, 76:182-191, 2020 Cited by PubMed Abstract: Casein kinase 2 (CK2) is a ubiquitous pleiotropic enzyme that is highly conserved across eukaryotic kingdoms. CK2 is singular amongst kinases as it is highly rigid and constitutively active. Arabidopsis thaliana is widely used as a model system in molecular plant research; the biological functions of A. thaliana CK2 are well studied in vivo and many of its substrates have been identified. Here, crystal structures of the α subunit of A. thaliana CK2 in three crystal forms and of its complex with the nonhydrolyzable ATP analog AMppNHp are presented. While the C-lobe of the enzyme is highly rigid, structural plasticity is observed for the N-lobe. Small but significant displacements within the active cleft are necessary in order to avoid steric clashes with the AMppNHp molecule. Binding of AMppNHp is influenced by a rigid-body motion of the N-lobe that was not previously recognized in maize CK2. PubMed: 32254052DOI: 10.1107/S2053230X20004537 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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