6Y69
Cryo-EM structure of an Escherichia coli 70S ribosome in complex with antibiotic TetracenomycinX
This is a non-PDB format compatible entry.
Summary for 6Y69
| Entry DOI | 10.2210/pdb6y69/pdb |
| EMDB information | 10705 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (56 entities in total) |
| Functional Keywords | tetracenomycin, ribosome |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 54 |
| Total formula weight | 2141149.23 |
| Authors | Wieland, M.,Wilson, D.N. (deposition date: 2020-02-26, release date: 2020-07-01, Last modification date: 2024-10-16) |
| Primary citation | Osterman, I.A.,Wieland, M.,Maviza, T.P.,Lashkevich, K.A.,Lukianov, D.A.,Komarova, E.S.,Zakalyukina, Y.V.,Buschauer, R.,Shiriaev, D.I.,Leyn, S.A.,Zlamal, J.E.,Biryukov, M.V.,Skvortsov, D.A.,Tashlitsky, V.N.,Polshakov, V.I.,Cheng, J.,Polikanov, Y.S.,Bogdanov, A.A.,Osterman, A.L.,Dmitriev, S.E.,Beckmann, R.,Dontsova, O.A.,Wilson, D.N.,Sergiev, P.V. Tetracenomycin X inhibits translation by binding within the ribosomal exit tunnel. Nat.Chem.Biol., 16:1071-1077, 2020 Cited by PubMed Abstract: The increase in multi-drug resistant pathogenic bacteria is making our current arsenal of clinically used antibiotics obsolete, highlighting the urgent need for new lead compounds with distinct target binding sites to avoid cross-resistance. Here we report that the aromatic polyketide antibiotic tetracenomycin (TcmX) is a potent inhibitor of protein synthesis, and does not induce DNA damage as previously thought. Despite the structural similarity to the well-known translation inhibitor tetracycline, we show that TcmX does not interact with the small ribosomal subunit, but rather binds to the large subunit, within the polypeptide exit tunnel. This previously unappreciated binding site is located adjacent to the macrolide-binding site, where TcmX stacks on the noncanonical basepair formed by U1782 and U2586 of the 23S ribosomal RNA. Although the binding site is distinct from the macrolide antibiotics, our results indicate that like macrolides, TcmX allows translation of short oligopeptides before further translation is blocked. PubMed: 32601485DOI: 10.1038/s41589-020-0578-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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