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Crystal structure of Arabidopsis thaliana casein kinase 2 alpha1

Journal Contribution - Journal Article

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 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.
Journal: Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
ISSN: 1744-3091
Issue: 4
Volume: 76
Pages: 182-191
Number of pages: 10
Publication year:2020
Keywords:X-ray crystallography, Protein structure, Macromolecular crystallography, Casein kinase 2, Structural Biology
Accessibility:Closed