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.
Original languageEnglish
Pages (from-to)182-191
Number of pages10
JournalActa Crystallogr F Struct Biol Commun
VolumeF76
Issue number4
DOIs
Publication statusPublished - 1 Apr 2020

    Research areas

  • X-ray crystallography, Protein structure, Macromolecular crystallography, Casein kinase 2, Structural Biology

ID: 51222757