7CHD

AtaT complexed with acetyl-methionyl-tRNAfMet

Summary for 7CHD

• Entry DOI: 10.2210/pdb7chd/pdb
• Descriptor: N-acetyltransferase domain-containing protein, RNA (77-MER) (2 entities in total)
• Functional Keywords: acetyltranferase, toxin, transferase
• Biological source: Escherichia coli O157:H7; More
• Total number of polymer chains: 10
• Total formula weight: 216312.00

Authors

Yashiro, Y.,Tomita, K. (deposition date: 2020-07-05, release date: 2020-11-04, Last modification date: 2023-11-29)

Primary citation

Yashiro, Y.,Sakaguchi, Y.,Suzuki, T.,Tomita, K.
Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli.
Nat Commun, 11:5438-5438, 2020

PubMed Abstract: Toxin-antitoxin systems in bacteria contribute to stress adaptation, dormancy, and persistence. AtaT, a type-II toxin in enterohemorrhagic E. coli, reportedly acetylates the α-amino group of the aminoacyl-moiety of initiator Met-tRNAf, thus inhibiting translation initiation. Here, we show that AtaT has a broader specificity for aminoacyl-tRNAs than initially claimed. AtaT efficiently acetylates Gly-tRNA, Trp-tRNA, Tyr-tRNA and Phe-tRNA isoacceptors, in addition to Met-tRNAf, and inhibits global translation. AtaT interacts with the acceptor stem of tRNAf, and the consecutive G-C pairs in the bottom-half of the acceptor stem are required for acetylation. Consistently, tRNA, tRNA, tRNA and tRNA also possess consecutive G-C base-pairs in the bottom halves of their acceptor stems. Furthermore, misaminoacylated valyl-tRNAf and isoleucyl-tRNAf are not acetylated by AtaT. Therefore, the substrate selection by AtaT is governed by the specific acceptor stem sequence and the properties of the aminoacyl-moiety of aminoacyl-tRNAs.

PubMed: 33116145
DOI: 10.1038/s41467-020-19281-z

Experimental method

X-RAY DIFFRACTION (3.804 Å)