2PVR: Crystal Structure Of The Catalytic Subunit Of Protein Kinase Ck2 (c- Terminal Deletion Mutant 1-335) In Complex With Two Sulfate Ions

CK2alpha is the catalytic subunit of protein kinase CK2 and a member of the CMGC family of eukaryotic protein kinases like the cyclin-dependent kinases, the MAP kinases and glycogen-synthase kinase 3. We present here a 1.6 A resolution crystal structure of a fully active C-terminal deletion mutant of human CK2alpha liganded by two sulfate ions, and we compare this structure systematically with representative structures of related CMGC kinases. The two sulfate anions occupy binding pockets at the activation segment and provide the structural basis of the acidic consensus sequence S/T-D/E-X-D/E that governs substrate recognition by CK2. The anion binding sites are conserved among those CMGC kinases. In most cases they are neutralized by phosphorylation of a neighbouring threonine or tyrosine side-chain, which triggers conformational changes for regulatory purposes. CK2alpha, however, lacks both phosphorylation sites at the activation segment and structural plasticity. Here the anion binding sites are functionally changed from regulation to substrate recognition. These findings underline the exceptional role of CK2alpha as a constitutively active enzyme within a family of strictly controlled protein kinases.
PDB ID: 2PVRDownload
MMDB ID: 47243
PDB Deposition Date: 2007/5/10
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 1.61  Å
Source Organism:
Similar Structures:
Biological Unit for 2PVR: monomeric; determined by author
Molecular Components in 2PVR
Label Count Molecule
Protein (1 molecule)
Casein Kinase II Subunit Alpha, Catalytic Subunit(Gene symbol: CSNK2A1)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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