Lysine-60 in copper chaperone Atox1 plays an essential role in adduct formation with a target Wilson disease domain

被引：0
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作者：
Hussain, Faiza [1 ]
Rodriguez-Granillo, Agustina [1 ]
Wittung-Stafshede, Pernilla [2 ]
机构：
[1] Department of Biochemistry and Cell Biology, Rice University, 6100 Main Street, Houston, TX 77251, United States
[2] Department of Chemistry, Chemical Biological Center, Umeå University, 901 87 Umeå, Sweden
来源：
Journal of the American Chemical Society | 2009年 / 131卷 / 45期
关键词：
(Figure Presented) 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 tool to probe chaperone-target interactions; in combination with gel 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. © 2009 American Chemical Society;
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Journal article (JA)
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页码：16371 / 16373
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