Literature summary extracted from
Niefind, K.; Guerra, B.; Pinna, L.A.; Issinger, O.G.; Schomburg, D.
Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution (1998), EMBO J., 17, 2451-2462.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.11.1 |
expression in Escherichia coli |
Zea mays |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.11.1 |
crystallized by vapour diffusion method. Crystal structure, at 2.1 A resolution, of recombinant alpha subunit of protein kinase CK2a in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents |
Zea mays |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.11.1 |
Zea mays |
P28523 |
casein kinase II subunit alpha |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.11.1 |
- |
Zea mays |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.11.1 |
CK2 |
- |
Zea mays |