Purification, crystallization and preliminary X-ray analysis of the DndE protein from Salmonella enterica serovar Cerro 87, which is involved in DNA phosphorothioation

被引：5

作者：

Chen, Fukun ^{[1
,2
]}

Lin, Kui ^{[1
,2
]}

Zhang, Zhenyi ^{[1
,2
]}

Chen, Leyi ^{[1
,2
]}

Shi, Xiaoshan ^{[1
,2
]}

Cao, Chunyang ^{[3
]}

Wang, Zhijun ^{[1
,2
]}

Liang, Jingdan ^{[1
,2
]}

Deng, Zixin ^{[1
,2
]}

Wu, Geng ^{[1
,2
]}

机构：

[1] Shanghai Jiao Tong Univ, State Key Lab Microbial Metab, Shanghai 200240, Peoples R China

[2] Shanghai Jiao Tong Univ, Sch Life Sci & Biotechnol, Shanghai 200240, Peoples R China

[3] Chinese Acad Sci, Shanghai Inst Organ Chem, Shanghai 200032, Peoples R China

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷

基金：

中国国家自然科学基金;

关键词：

STREPTOMYCES-LIVIDANS; SULFUR; BACKBONE; IRON;

D O I：

10.1107/S1744309111036694

中图分类号：

Q5 [生物化学];

学科分类号：

070307 [化学生物学];

摘要：

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.

引用

收藏

页码：1440 / 1442

页数：3

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