期刊
STRUCTURE
卷 27, 期 3, 页码 476-+出版社
CELL PRESS
DOI: 10.1016/j.str.2018.11.005
关键词
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资金
- JSPS [18H03980]
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [26113002]
- Takeda Science Foundation
- Japan Foundation for Applied Enzymology
- Terumo Foundation for Life Science and Art
- Princess Takamatsu Cancer Research Fund
- Grants-in-Aid for Scientific Research [26113002, 18H03980] Funding Source: KAKEN
AtaT-AtaR is an enterohemorrhagic Escherichia coli toxin-antitoxin system that modulates cellular growth under stress conditions. AtaT and AtaR act as a toxin and its repressor, respectively. AtaT is a member of the GNAT family, and the dimeric AtaT acetylates the alpha-amino group of the aminoacyl moiety of methionyl initiator tRNA(fMet), thereby inhibiting translation initiation. The crystallographic analysis of the AtaT-AtaR complex revealed that the AtaT-AtaR proteins form a heterohexameric [AtaT-(AtaR(4))-AtaT] complex, where two V-shaped AtaR dimers bridge two AtaT molecules. The N-terminal region of AtaR is required for its dimerization, and the C-terminal region of AtaR interacts with AtaT. The two AtaT molecules are spatially separated in the AtaT-AtaR complex. AtaT alone forms a dimer in solution, which is enzymatically active. The present structure, in which AtaR prevents AtaT from forming an active dimer, reveals the molecular basis of the AtaT toxicity repression by the antitoxin AtaR.
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