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Structure of the Type VI Effector-Immunity Complex (Tae4-Tai4) Provides Novel Insights into the Inhibition Mechanism of the Effector by Its Immunity Protein
Zhang H(张衡); Zhang, H; 高增强; Zhang, H; Gao, ZQ; Wang, WJ; Liu, GF; Xu, JH; Su, XD; Dong, YH;; Wang WJ(王文佳); Liu GF(刘广峰); Xu JH(徐建华); Dong YH(董宇辉)
2013
发表期刊JOURNAL OF BIOLOGICAL CHEMISTRY
卷号288期号:8页码:5928-5939
摘要The type VI secretion system (T6SS), a multisubunit needle-like apparatus, has recently been found to play a role in interspecies interactions. The Gram-negative bacteria harboring T6SS (donor) deliver the effectors into their neighboring cells (recipient) to kill them. Meanwhile, the cognate immunity proteins were employed to protect the donor cells against the toxic effectors. Tae4 (type VI amidase effector 4) and Tai4 (type VI amidase immunity 4) are newly identified T6SS effector-immunity pairs. Here, we report the crystal structures of Tae4 from Enterobacter cloacae and Tae4-Tai4 complexes from both E. cloacae and Salmonella typhimurium. Tae4 acts as a DL-endopeptidase and displays a typical N1pC/P60 domain. Unlike Tsi1 (type VI secretion immunity 1), Tai4 is an all-helical protein and forms a dimer in solution. The small angle x-ray scattering study combined with the analytical ultracentrifugation reveal that the Tae4-Tai4 complex is a compact heterotetramer that consists of a Tai4 dimer and two Tae4 molecules in solution. Structure-based mutational analysis of the Tae4-Tai4 interface shows that a helix (alpha 3) of one subunit in dimeric Tai4 plays a major role in binding of Tae4, whereas a protruding loop (L4) in the other subunit is mainly responsible for inhibiting Tae4 activity. The inhibition process requires collaboration between the Tai4 dimer. These results reveal a novel and unique inhibition mechanism in effector-immunity pairs and suggest a new strategy to develop antipathogen drugs.
学科领域Biochemistry & Molecular Biology
DOI10.1074/jbc.M112.434357
收录类别SCI
WOS记录号WOS:000315342500061
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被引频次:28[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/224271
专题多学科研究中心
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Zhang H,Zhang, H,高增强; Zhang, H,et al. Structure of the Type VI Effector-Immunity Complex (Tae4-Tai4) Provides Novel Insights into the Inhibition Mechanism of the Effector by Its Immunity Protein[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2013,288(8):5928-5939.
APA 张衡.,Zhang, H.,高增强; Zhang, H.,Gao, ZQ.,Wang, WJ.,...&董宇辉.(2013).Structure of the Type VI Effector-Immunity Complex (Tae4-Tai4) Provides Novel Insights into the Inhibition Mechanism of the Effector by Its Immunity Protein.JOURNAL OF BIOLOGICAL CHEMISTRY,288(8),5928-5939.
MLA 张衡,et al."Structure of the Type VI Effector-Immunity Complex (Tae4-Tai4) Provides Novel Insights into the Inhibition Mechanism of the Effector by Its Immunity Protein".JOURNAL OF BIOLOGICAL CHEMISTRY 288.8(2013):5928-5939.
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