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Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.

ABSTRACT: CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) 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 close interaction between the N-terminal region and the activation segment is unique among known protein kinase structures and probably contributes to the constitutively active nature of CK2. 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.

SUBMITTER: Niefind K

PROVIDER: S-EPMC1170587 | biostudies-other | 1998 May

REPOSITORIES: biostudies-other

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Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.

Niefind K K Guerra B B Pinna L A LA Issinger O G OG Schomburg D D

The EMBO journal 19980501 9

CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) 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 close interaction bet ...[more]

PMID: 9564028

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