The crystal structure of the complex of Zea mays α subunit with a fragment of human β subunit provides the clue to the architecture of protein kinase CK2 holoenzyme

被引:29
作者
Battistutta, R
Sarno, S
De Moliner, E
Marin, O
Issinger, OG
Zanotti, G
Pinna, LA
机构
[1] Univ Padua, Dept Organ Chem, I-35131 Padua, Italy
[2] Univ Padua, CNR, Biopolymer Res Ctr, I-35131 Padua, Italy
[3] Univ Padua, CNR, Biomembrane Res Ctr, I-35131 Padua, Italy
[4] Univ Padua, Dept Biol Chem, I-35131 Padua, Italy
[5] Syddansk Univ, Biokemisk Inst, Odense, Denmark
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 2000年 / 267卷 / 16期
关键词
CK2; phosphorylation; protein kinase; crystal structure; holoenzyme;
D O I
10.1046/j.1432-1327.2000.01587.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The crystal structure of a complex between the catalytic or 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-Angstrom 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 alpha(2) 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.
引用
收藏
页码:5184 / 5190
页数:7
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