Structural and saxs analysis of tle5-tli5 complex reveals a novel inhibition mechanism of h2-t6ss in pseudomonas aeruginosa
文献类型：期刊论文
| 作者 | Yang, Xiao-Yun1; Li, Zong-Qiang2; Gao, Zeng-Qiang3; Wang, Wen-Jia4; Geng, Zhi3; Xu, Jian-Hua3; She, Zhun3; Dong, Yu-Hui3 |
| 刊名 | Protein science
 |
| 出版日期 | 2017-10-01 |
| 卷号 | 26期号:10页码:2083-2091 |
| 关键词 | X-ray crystallography Saxs Immunity protein Type vi secretion system |
| ISSN号 | 0961-8368 |
| DOI | 10.1002/pro.3246 |
| 通讯作者 | She, zhun(shezhun@ihep.ac.cn) ; Dong, yu-hui(dongyh@ihep.ac.cn) |
| 英文摘要 | Widely spread in gram-negative bacteria, the type vi secretion system (t6ss) secretes many effector-immunity protein pairs to help the bacteria compete against other prokaryotic rivals, and infect their eukaryotic hosts. tle5 and tle5b are two phospholipase effector protein secreted by t6ss of pseudomonas aeruginosa. they can facilitate the bacterial internalization process into human epithelial cells by interacting with akt protein of the pi3k-akt signal pathway. tli5 and pa5086-5088 are cognate immunity proteins of tle5 and tle5b, respectively. they can interact with their cognate effector proteins to suppress their virulence. here, we report the crystal structure of tli5 at 2.8 angstrom resolution and successfully fit it into the small angle x-ray scattering (saxs) model of the complete tle5-tli5 complex. we identified two important motifs in tli5 through sequence and structural analysis. one is a conserved loop--hairpin motif that exists in the tle5 immunity homologs, the other is a long and sharp - motif that directly interacts with tle5 according to saxs data. we also distinguished the structural features of tle5 and tle5b family immunity proteins. together, our work provided insights into a novel inhibition mechanism that may enhance our understanding of phospholipase d family proteins. |
| WOS关键词 | SELF-PROTECTION MECHANISM ; SECRETION SYSTEM ; PROTEIN ; MODEL ; PHOSPHOLIPASES ; SCATTERING ; EFFECTORS ; MEMBRANE ; INSIGHTS ; ENCODES |
| WOS研究方向 | Biochemistry & Molecular Biology |
| WOS类目 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000411179200017 |
| 出版者 | WILEY |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2177080 |
| 专题 | 高能物理研究所 |
| 通讯作者 | She, Zhun; Dong, Yu-Hui |
| 作者单位 | 1.Univ Sci & Technol China, Sch Life Sci, Key Lab Struct Biol, Hefei, Anhui, Peoples R China 2.Chinese Acad Sci, Inst Biophys, Key Lab RNA Biol, Beijing, Peoples R China 3.Chinese Acad Sci, Inst High Energy Phys, Multidiscipline Res Ctr, Beijing 100049, Peoples R China 4.Qilu Univ Technol, Sch Sci, Dept Optoelect Informat, Jinan, Shandong, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Xiao-Yun,Li, Zong-Qiang,Gao, Zeng-Qiang,et al. Structural and saxs analysis of tle5-tli5 complex reveals a novel inhibition mechanism of h2-t6ss in pseudomonas aeruginosa[J]. Protein science,2017,26(10):2083-2091. |
| APA | Yang, Xiao-Yun.,Li, Zong-Qiang.,Gao, Zeng-Qiang.,Wang, Wen-Jia.,Geng, Zhi.,...&Dong, Yu-Hui.(2017).Structural and saxs analysis of tle5-tli5 complex reveals a novel inhibition mechanism of h2-t6ss in pseudomonas aeruginosa.Protein science,26(10),2083-2091. |
| MLA | Yang, Xiao-Yun,et al."Structural and saxs analysis of tle5-tli5 complex reveals a novel inhibition mechanism of h2-t6ss in pseudomonas aeruginosa".Protein science 26.10(2017):2083-2091. |
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来源：高能物理研究所
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