1DS5

DIMERIC CRYSTAL STRUCTURE OF THE ALPHA SUBUNIT IN COMPLEX WITH TWO BETA PEPTIDES MIMICKING THE ARCHITECTURE OF THE TETRAMERIC PROTEIN KINASE CK2 HOLOENZYME.

1DS5 の概要

• エントリーDOI: 10.2210/pdb1ds5/pdb
• 関連するPDBエントリー: 1A6O
• 分子名称: CASEIN KINASE, ALPHA CHAIN, CASEIN KINASE, BETA CHAIN, ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: protein-complex, tetramer, transferase
• 由来する生物種: Zea mays; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 169715.74

構造登録者

Battistutta, R.,Sarno, S.,De Moliner, E.,Marin, O.,Zanotti, G.,Pinna, L.A. (登録日: 2000-01-07, 公開日: 2001-01-07, 最終更新日: 2024-02-07)

主引用文献

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

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: 10931203
DOI: 10.1046/j.1432-1327.2000.01587.x

実験手法

X-RAY DIFFRACTION (3.16 Å)