8FR3
E. coli EF-Tu in complex with KKL-55
Summary for 8FR3
| Entry DOI | 10.2210/pdb8fr3/pdb |
| Descriptor | Elongation factor Tu, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | ef-tu, translation, antibiotic |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 90027.93 |
| Authors | Nguyen, H.A.,Kuzmishin Nagy, A.B.,Dunham, C.M. (deposition date: 2023-01-06, release date: 2023-09-20, Last modification date: 2023-11-29) |
| Primary citation | Marathe, N.,Nguyen, H.A.,Alumasa, J.N.,Kuzmishin Nagy, A.B.,Vazquez, M.,Dunham, C.M.,Keiler, K.C. Antibiotic that inhibits trans -translation blocks binding of EF-Tu to tmRNA but not to tRNA. Mbio, 14:e0146123-e0146123, 2023 Cited by PubMed Abstract: Elongation factor thermo-unstable (EF-Tu) is a universally conserved translation factor that mediates productive interactions between tRNAs and the ribosome. In bacteria, EF-Tu also delivers transfer-messenger RNA (tmRNA)-SmpB to the ribosome during -translation. We report the first small molecule, KKL-55, that specifically inhibits EF-Tu activity in -translation without affecting its activity in normal translation. KKL-55 has broad-spectrum antibiotic activity, suggesting that compounds targeted to the tmRNA-binding interface of EF-Tu could be developed into new antibiotics to treat drug-resistant infections. PubMed: 37681945DOI: 10.1128/mbio.01461-23 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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