1DS5
DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.
Summary for 1DS5
| Entry DOI | 10.2210/pdb1ds5/pdb |
| Related | 1A6O |
| Descriptor | CASEIN KINASE, ALPHA CHAIN, CASEIN KINASE, BETA CHAIN, ADENOSINE MONOPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | protein-complex, tetramer, transferase |
| Biological source | Zea mays More |
| Total number of polymer chains | 8 |
| Total formula weight | 169715.74 |
| Authors | Battistutta, R.,Sarno, S.,De Moliner, E.,Marin, O.,Zanotti, G.,Pinna, L.A. (deposition date: 2000-01-07, release date: 2001-01-07, Last modification date: 2024-02-07) |
| Primary citation | Battistutta, R.,Sarno, S.,De Moliner, E.,Marin, O.,Issinger, O.G.,Zanotti, G.,Pinna, L.A. The crystal structure of the complex of Zea mays alpha subunit with a fragment of human beta subunit provides the clue to the architecture of protein kinase CK2 holoenzyme. Eur.J.Biochem., 267:5184-5190, 2000 Cited by PubMed Abstract: The crystal structure of a complex between the catalytic alpha subunit of Zea mays CK2 and a 23-mer peptide corresponding the C-terminal sequence 181-203 of the human CK2 regulatory beta subunit has been determined at 3.16-A resolution. The complex, composed of two alpha chains and two peptides, presents a molecular twofold axis, with each peptide interacting with both alpha chains. In the derived model of the holoenzyme, the regulatory subunits are positioned on the opposite side with respect to the opening of the catalytic sites, that remain accessible to substrates and cosubstrates. The beta subunit can influence the catalytic activity both directly and by promoting the formation of the alpha2 dimer, in which each alpha chain interacts with the active site of the other. Furthermore, the two active sites are so close in space that they can simultaneously bind and phosphorylate two phosphoacceptor residues of the same substrate. PubMed: 10931203DOI: 10.1046/j.1432-1327.2000.01587.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.16 Å) |
Structure validation
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