7ZTA
Structure of an Escherichia coli 70S ribosome stalled by Tetracenomycin X during translation of an MAAAPQK(C) peptide
This is a non-PDB format compatible entry.
Summary for 7ZTA
| Entry DOI | 10.2210/pdb7zta/pdb |
| EMDB information | 14956 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (64 entities in total) |
| Functional Keywords | antibiotic, translation, ribosome, tetracenomycin x, protein synthesis inhibitor |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 57 |
| Total formula weight | 2202995.77 |
| Authors | Leroy, E.C.,Perry, T.N.,Renault, T.T.,Innis, C.A. (deposition date: 2022-05-09, release date: 2023-04-12, Last modification date: 2024-09-25) |
| Primary citation | Leroy, E.C.,Perry, T.N.,Renault, T.T.,Innis, C.A. Tetracenomycin X sequesters peptidyl-tRNA during translation of QK motifs. Nat.Chem.Biol., 19:1091-1096, 2023 Cited by PubMed 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-tRNA 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. PubMed: 37322159DOI: 10.1038/s41589-023-01343-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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