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- W4380714897 abstract "As antimicrobial resistance threatens our ability to treat common bacterial infections, new antibiotics with limited cross-resistance are urgently needed. In this regard, natural products that target the bacterial ribosome have the potential to be developed into potent drugs through structure-guided design, provided their mechanisms of action are well understood. Here we use inverse toeprinting coupled to next-generation sequencing to show that the aromatic polyketide tetracenomycin X primarily inhibits peptide bond formation between an incoming aminoacyl-tRNA and a terminal Gln-Lys (QK) motif in the nascent polypeptide. Using cryogenic electron microscopy, we reveal that translation inhibition at QK motifs occurs via an unusual mechanism involving sequestration of the 3′ adenosine of peptidyl-tRNALys in the drug-occupied nascent polypeptide exit tunnel of the ribosome. Our study provides mechanistic insights into the mode of action of tetracenomycin X on the bacterial ribosome and suggests a path forward for the development of novel aromatic polyketide antibiotics. Biochemical and structural analyses reveal how tetracenomycin X inhibits bacterial translation in a context-dependent manner that relies primarily on the presence of Gln-Lys motifs in the nascent polypeptide chain." @default.
- W4380714897 created "2023-06-15" @default.
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- W4380714897 date "2023-06-15" @default.
- W4380714897 modified "2023-09-24" @default.
- W4380714897 title "Tetracenomycin X sequesters peptidyl-tRNA during translation of QK motifs" @default.
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- W4380714897 doi "https://doi.org/10.1038/s41589-023-01343-0" @default.
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