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首页> 外文期刊>Nature structural biology >Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATpase
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Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATpase

机译：Menkes铜转运ATpase的第四个金属结合域的溶液结构

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摘要

Menkes disease is an X-linked disorder in copper transport that results in death during early childhood. The solution structures of both apo and Ag(I)-bound forms of the fourth metal-binding domain (mbd4) from the Menkes copper-transporting ATPase have been solved. The 72-residue mbd4 has a ferredoxin-like beta alpha beta beta alpha beta fold. Structural differences between the two forms are limited to the metal-binding loop, which is disordered in the apo structure but well ordered in the Ag(I)-bound structure. Ag(I) binds in a linear bicoordinate manner to the two Cys residues of the conserved GMTCxxC motif; Cu(I) likely coordinates in a similar manner. Menkes mbd4 is thus the first bicoordinate copper-binding protein to be characterized structurally. Sequence comparisons with other heavy-metal-binding domains reveal a conserved hydrophobic core and metal-binding motif. [References: 44]
机译：Menkes病是铜运输中与X连锁的疾病，可导致儿童早期死亡。解决了来自Menkes铜转运ATPase的第四种金属结合域（mbd4）的apo和Ag（I）结合形式的溶液结构。 72个残基的mbd4具有类似铁氧还蛋白的beta alpha beta beta alpha beta折叠。两种形式之间的结构差异仅限于金属结合环，其在apo结构中无序，但在与Ag（I）结合的结构中排列良好。 Ag（I）以线性双配位方式与保守的GMTCxxC基序的两个Cys残基结合; Cu（I）可能以相似的方式进行配位。因此，Menkes mbd4是第一个在结构上得到表征的双配位铜结合蛋白。与其他重金属结合域的序列比较揭示了保守的疏水核和金属结合基序。 [参考：44]

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