6AJM

Crystal structure of apo AtaTR

Summary for 6AJM

• Entry DOI: 10.2210/pdb6ajm/pdb
• Descriptor: N-acetyltransferase, DUF1778 domain-containing protein, TRIETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: toxin, antitoxin, acetyltransferase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 6
• Total formula weight: 81396.96

Authors

Yashiro, Y.,Yamashita, S.,Tomita, K. (deposition date: 2018-08-28, release date: 2019-01-02, Last modification date: 2023-11-22)

Primary citation

Yashiro, Y.,Yamashita, S.,Tomita, K.
Crystal Structure of the Enterohemorrhagic Escherichia coli AtaT-AtaR Toxin-Antitoxin Complex.
Structure, 27:476-, 2019

PubMed Abstract: 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 α-amino group of the aminoacyl moiety of methionyl initiator tRNA, thereby inhibiting translation initiation. The crystallographic analysis of the AtaT-AtaR complex revealed that the AtaT-AtaR proteins form a heterohexameric [AtaT-(AtaR)-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.

PubMed: 30612860
DOI: 10.1016/j.str.2018.11.005

Experimental method

X-RAY DIFFRACTION (2.604 Å)