Lysine-60 in Copper Chaperone Atox1 Plays an Essential Role in Adduct Formation with a Target Wilson Disease Domain

被引：40

作者：

Hussain, Faiza ^{[2
]}

Rodriguez-Granillo, Agustina ^{[2
]}

Wittung-Stafshede, Pernilla ^{[1
]}

机构：

[1] Umea Univ, Dept Chem, Chem Biol Ctr, S-90187 Umea, Sweden

[2] Rice Univ, Dept Biochem & Cell Biol, Houston, TX 77251 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2009年 / 131卷 / 45期

关键词：

PROTEIN; METALLOCHAPERONE; DYNAMICS; HAH1;

D O I：

10.1021/ja9058266

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The mechanism by which the human copper (Cu) chaperone Atox1 delivers Cu to metal-binding domains of Wilson disease (WD) protein for insertion into cuproenzymes is unclear. Using near-UV circular dichroism as a new too[ to probe chaperone-target interactions, in combination with get filtration and molecular dynamics simulations, we here demonstrate that Atox1 forms a stable Cu-dependent adduct with the fourth metal-binding domain of WD (WD4). Using point-mutated Atox1 variants, we show that the adduct forms in the absence of conserved residues M10 or T11 but K60 is essential for heterocomplex formation and Cu transfer. Dissection of heterocomplex energetic components reveals a crucial role for K60- mediated electrostatic interaction.

引用

页码：16371 / +

页数：5

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