7chd | pdb_00007chd

AtaT complexed with acetyl-methionyl-tRNAfMet

spinqualitylabelsall models 7chd, resolution 3.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7chd is a 10 chain structure with sequence from Escherichia coli and Escherichia coli O157:H7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.804Å Ligands: 4SU, 5MU, H2U, OMC, PSU Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8XED1_ECO57 Publication Abstract from PubMed Toxin-antitoxin systems in bacteria contribute to stress adaptation, dormancy, and persistence. AtaT, a type-II toxin in enterohemorrhagic E. coli, reportedly acetylates the alpha-amino group of the aminoacyl-moiety of initiator Met-tRNAf(Met), thus inhibiting translation initiation. Here, we show that AtaT has a broader specificity for aminoacyl-tRNAs than initially claimed. AtaT efficiently acetylates Gly-tRNA(Gly), Trp-tRNA(Trp), Tyr-tRNA(Tyr) and Phe-tRNA(Phe) isoacceptors, in addition to Met-tRNAf(Met), and inhibits global translation. AtaT interacts with the acceptor stem of tRNAf(Met), and the consecutive G-C pairs in the bottom-half of the acceptor stem are required for acetylation. Consistently, tRNA(Gly), tRNA(Trp), tRNA(Tyr) and tRNA(Phe) also possess consecutive G-C base-pairs in the bottom halves of their acceptor stems. Furthermore, misaminoacylated valyl-tRNAf(Met) and isoleucyl-tRNAf(Met) 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. Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli.,Yashiro Y, Sakaguchi Y, Suzuki T, Tomita K Nat Commun. 2020 Oct 28;11(1):5438. doi: 10.1038/s41467-020-19281-z. PMID:33116145 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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