Purification, crystallization and preliminary X-ray analysis of the DndE protein from Salmonella enterica serovar Cerro 87, which is involved in DNA phosphorothioation
Purification, crystallization and preliminary X-ray analysis of the DndE protein from Salmonella enterica serovar Cerro 87, which is involved in DNA phosphorothioation
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肠沙门氏菌 Cerro 87 血清型 DndE 蛋白的纯化、结晶和初步 X 射线分析，该蛋白参与 DNA 硫代磷酸化
DOI：
10.1107/s1744309111036694
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发表时间：
2011-11-01
影响因子：
0.9
通讯作者：
Wu, Geng
中科院分区：
文献类型：
--
作者：
Chen, Fukun;Lin, Kui;Wu, Geng
DNA硫代磷酸化（DNA硫修饰）现象在原核生物中广泛存在，可能是限制细菌间基因转移的一种机制。DndE是DNA硫代磷酸化过程所需的五种必需蛋白质之一。然而，其在DNA硫修饰中的确切生物化学作用仍不清楚。在这项研究中，DndE蛋白同源物从沙门氏菌Cerro 87血清型过表达，纯化和结晶。DndE蛋白的晶体衍射至2.7埃分辨率，属于空间群P3（1）21。这些结果将有助于详细的结构分析DndE和进一步阐明其生化功能。
The phenomenon of DNA phosphorothioation (DNA sulfur modification) is widespread among prokaryotes and may serve as a mechanism to restrict gene transfer among bacteria. DndE is one of five essential proteins that are required for the DNA phosphorothioation process. However, its exact biochemical role in sulfur modification of DNA remains unclear. In this study, the DndE protein homologue from Salmonella enterica serovar Cerro 87 was overexpressed, purified and crystallized. The crystals of the DndE protein diffracted to 2.7 angstrom resolution and belonged to space group P3(1)21. These results will facilitate detailed structural analysis of DndE and further elucidation of its biochemical function.