The 1.4 Ã… Crystal Structure of the ArsD Arsenic Metallochaperone Provides Insights into Its interaction with the ArsA ATPase
The 1.4 Ã… Crystal Structure of the ArsD Arsenic Metallochaperone Provides Insights into Its interaction with the ArsA ATPase
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DOI：
10.1021/bi100571r
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发表时间：
2010-06-29
期刊：
影响因子：
2.9
通讯作者：
Rosen, Barry P.
中科院分区：
文献类型：
--
作者：
Ye, Jun;Ajees, A. Abdul;Rosen, Barry P.
砷是一种致癌物质，在超级基金的危险化学品清单上名列前茅。细菌对砷的抗性是由ArsD促进的，ArsD将As（III）递送到ArsA ATP酶，ArsAB泵的催化亚基。在这里，我们报告的砷金属伴侣ArsD在1.4埃的结构和模型，其结合的类金属。在不对称单元中有两个ArsD分子。ArsD单体的整体结构具有硫氧还蛋白折叠，其核心为四条β-链，两侧为四条α-螺旋。基于结构同源物的数据，ArsD建模和不绑定的As（III）。ArsD结合每个单体一个砷，与Cys 12、Cys 13和Cys 18的三个硫原子配位。使用该结构模型，使用算法对接ArsD和ArsA。由此产生的对接模型提供了两种蛋白质的接触点的可测试的预测，并形成了未来实验的基础。
Arsenic is a carcinogen that tops the Superfund list of hazardous chemicals. Bacterial resistance to arsenic is facilitated by ArsD, which delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump. Here we report the structure of the arsenic metallochaperone ArsD at 1.4 angstrom and a model for its binding of metalloid. There are two ArsD molecules in the asymmetric unit. The overall structure of the ArsD monomer has a thioredoxin fold, with a core of four beta-strands flanked by four alpha-helices. Based on data from structural homologues, ArsD was modeled with and without bound As(III). ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13, and Cys18. Using this structural model, an algorithm was used to dock ArsD and ArsA. The resulting docking model provides testable predictions of the contact points of the two proteins and forms the basis for future experiments.