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Literature summary for 2.7.11.1 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Zea mays

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Zea mays P28523 casein kinase II subunit alpha
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Purification (Commentary)

Purification (Comment) Organism
-
Zea mays

Synonyms

Synonyms Comment Organism
CK2
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Zea mays