| Structural highlights
6xx7 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.4Å |
| Ligands: | ANP, CL, MG, PGE, SO4 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CSK21_ARATH Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates casein in vitro (PubMed:7678767). The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor GBFl, resulting in stimulation of its DNA binding activity (PubMed:7696877). CK2 phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis (PubMed:21330376). CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation (PubMed:19509278, PubMed:19509420). Acts as circadian clock component that maintains the correct period length through phosphorylation of CCA1 (PubMed:21900482). Required for the maintenance and control of genomic stability and chromatin structure (PubMed:22487192). May act as an ectokinase that phosphorylates several extracellular proteins.[1] [2] [3] [4] [5] [6] [7]
Publication Abstract from PubMed
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 alpha 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.
Crystal structure of Arabidopsis thaliana casein kinase 2 alpha1.,Demulder M, De Veylder L, Loris R Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):182-191. doi:, 10.1107/S2053230X20004537. Epub 2020 Apr 6. PMID:32254052[8]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dennis MD, Browning KS. Differential phosphorylation of plant translation initiation factors by Arabidopsis thaliana CK2 holoenzymes. J Biol Chem. 2009 Jul 31;284(31):20602-14. doi: 10.1074/jbc.M109.006692. Epub, 2009 Jun 9. PMID:19509278 doi:https://dx.doi.org/10.1074/jbc.M109.006692
- ↑ Dennis MD, Person MD, Browning KS. Phosphorylation of plant translation initiation factors by CK2 enhances the in vitro interaction of multifactor complex components. J Biol Chem. 2009 Jul 31;284(31):20615-28. Epub 2009 Jun 9. PMID:19509420 doi:https://dx.doi.org/M109.007658
- ↑ Bu Q, Zhu L, Dennis MD, Yu L, Lu SX, Person MD, Tobin EM, Browning KS, Huq E. Phosphorylation by CK2 enhances the rapid light-induced degradation of phytochrome interacting factor 1 in Arabidopsis. J Biol Chem. 2011 Apr 8;286(14):12066-74. doi: 10.1074/jbc.M110.186882. Epub 2011, Feb 17. PMID:21330376 doi:https://dx.doi.org/10.1074/jbc.M110.186882
- ↑ Lu SX, Liu H, Knowles SM, Li J, Ma L, Tobin EM, Lin C. A role for protein kinase casein kinase2 alpha-subunits in the Arabidopsis circadian clock. Plant Physiol. 2011 Nov;157(3):1537-45. doi: 10.1104/pp.111.179846. Epub 2011 Sep, 7. PMID:21900482 doi:https://dx.doi.org/10.1104/pp.111.179846
- ↑ Moreno-Romero J, Armengot L, Mar Marques-Bueno M, Britt A, Carmen Martinez M. CK2-defective Arabidopsis plants exhibit enhanced double-strand break repair rates and reduced survival after exposure to ionizing radiation. Plant J. 2012 Aug;71(4):627-38. doi: 10.1111/j.1365-313X.2012.05019.x. Epub 2012 , Jun 11. PMID:22487192 doi:https://dx.doi.org/10.1111/j.1365-313X.2012.05019.x
- ↑ Mizoguchi T, Yamaguchi-Shinozaki K, Hayashida N, Kamada H, Shinozaki K. Cloning and characterization of two cDNAs encoding casein kinase II catalytic subunits in Arabidopsis thaliana. Plant Mol Biol. 1993 Jan;21(2):279-89. PMID:7678767
- ↑ Klimczak LJ, Collinge MA, Farini D, Giuliano G, Walker JC, Cashmore AR. Reconstitution of Arabidopsis casein kinase II from recombinant subunits and phosphorylation of transcription factor GBF1. Plant Cell. 1995 Jan;7(1):105-15. doi: 10.1105/tpc.7.1.105. PMID:7696877 doi:https://dx.doi.org/10.1105/tpc.7.1.105
- ↑ Demulder M, De Veylder L, Loris R. Crystal structure of Arabidopsis thaliana casein kinase 2 α1. Acta Crystallogr F Struct Biol Commun. 2020 Apr 1;76(Pt 4):182-191. PMID:32254052 doi:10.1107/S2053230X20004537
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