中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Structural analysis of the regulatory mechanism of marr protein rv2887 in m-tuberculosis

文献类型:期刊论文

作者Gao, Yun-Rong1,2,3,9; Li, De-Feng2,3; Fleming, Joy1,2,3; Zhou, Ya-Feng1; Liu, Ying4; Deng, Jiao-Yu5; Zhou, Lin6; Zhou, Jie7; Zhu, Guo-Feng2,3; Zhang, Xian-En2,3
刊名Scientific reports
出版日期2017-07-25
卷号7页码:13
ISSN号2045-2322
DOI10.1038/s41598-017-01705-4
通讯作者Wang, da-cheng(dcwang@ibp.ac.cn) ; Bi, li-jun(blj@ibp.ac.cn)
英文摘要Marr family proteins are transcriptional regulators that control expression of bacterial proteins involved in metabolism, virulence, stress responses and multi-drug resistance, mainly via ligandmediated attenuation of dna binding. greater understanding of their underlying regulatory mechanism may open up new avenues for the effective treatment of bacterial infections. to gain molecular insight into the mechanism of rv2887, a marr family protein in m. tuberculosis, we first showed that it binds salicylate (sa) and para-aminosalicylic acid (pas), its structural analogue and an antitubercular drug, in a 1: 1 stoichiometry with high affinity. subsequent determination and analysis of rv2887 crystal structures in apo form, and in complex with sa, pas and dna showed that sa and pas bind to rv2887 at similar sites, and that rv2887 interacts with dna mainly by insertion of helix alpha 4 into the major groove. ligand binding triggers rotation of the whth domain of rv2887 toward the dimerization domain, causing changes in protein conformation such that it can no longer bind to a 27 bp recognition sequence in the upstream region of gene rv0560c. the structures provided here lay a foundation for the design of small molecules that target rv2887, a potential new approach for the development of anti-mycobacterials.
WOS关键词FAMILY TRANSCRIPTIONAL REGULATOR ; DNA-BINDING MECHANISM ; MULTIPLE ANTIBIOTIC-RESISTANCE ; CRYSTAL-STRUCTURE REVEALS ; ESCHERICHIA-COLI ; VIRULENCE ; NETWORK ; GENE ; TETRACYCLINE ; EXPRESSION
WOS研究方向Science & Technology - Other Topics
WOS类目Multidisciplinary Sciences
语种英语
WOS记录号WOS:000406281400036
出版者NATURE PUBLISHING GROUP
URI标识http://www.irgrid.ac.cn/handle/1471x/2373365
专题武汉病毒研究所
通讯作者Wang, Da-Cheng; Bi, Li-Jun
作者单位1.Foshan Univ, Sch Stomatol & Med, Foshan 528000, Guangdong, Peoples R China
2.Chinese Acad Sci, Key Lab RNA Biol, Beijing 100101, Peoples R China
3.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China
4.East China Univ Sci & Technol, Sch Pharm, Shanghai Key Lab New Drug Design, Shanghai 200237, Peoples R China
5.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Hubei, Peoples R China
6.Ctr TB Control Guangdong Prov, Guangzhou 51630, Guangdong, Peoples R China
7.4th Peoples Hosp, Foshan 528000, Guangdong, Peoples R China
8.Guangdong Prov Key Lab TB Syst Biol & Translat M, Foshan 528000, Guangdong, Peoples R China
9.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714
Gao, Yun-Rong,Li, De-Feng,Fleming, Joy,et al. Structural analysis of the regulatory mechanism of marr protein rv2887 in m-tuberculosis[J]. Scientific reports,2017,7:13.
APA Gao, Yun-Rong.,Li, De-Feng.,Fleming, Joy.,Zhou, Ya-Feng.,Liu, Ying.,...&Bi, Li-Jun.(2017).Structural analysis of the regulatory mechanism of marr protein rv2887 in m-tuberculosis.Scientific reports,7,13.
MLA Gao, Yun-Rong,et al."Structural analysis of the regulatory mechanism of marr protein rv2887 in m-tuberculosis".Scientific reports 7(2017):13.

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来源:武汉病毒研究所

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