5AFI
2.9A Structure of E. coli ribosome-EF-TU complex by cs-corrected cryo-EM
This is a non-PDB format compatible entry.
Summary for 5AFI
| Entry DOI | 10.2210/pdb5afi/pdb |
| EMDB information | 2847 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (66 entities in total) |
| Functional Keywords | ribosome, translation, protein synthesis, decoding, elongation factor tu, trna, rna modification, antibiotic |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 59 |
| Total formula weight | 2302707.49 |
| Authors | Fischer, N.,Neumann, P.,Konevega, A.L.,Bock, L.V.,Ficner, R.,Rodnina, M.V.,Stark, H. (deposition date: 2015-01-22, release date: 2015-03-11, Last modification date: 2025-03-12) |
| Primary citation | Fischer, N.,Neumann, P.,Konevega, A.L.,Bock, L.V.,Ficner, R.,Rodnina, M.V.,Stark, H. Structure of the E. coli ribosome-EF-Tu complex at <3 angstrom resolution by Cs-corrected cryo-EM. Nature, 520:567-570, 2015 Cited by PubMed Abstract: Single particle electron cryomicroscopy (cryo-EM) has recently made significant progress in high-resolution structure determination of macromolecular complexes due to improvements in electron microscopic instrumentation and computational image analysis. However, cryo-EM structures can be highly non-uniform in local resolution and all structures available to date have been limited to resolutions above 3 Å. Here we present the cryo-EM structure of the 70S ribosome from Escherichia coli in complex with elongation factor Tu, aminoacyl-tRNA and the antibiotic kirromycin at 2.65-2.9 Å resolution using spherical aberration (Cs)-corrected cryo-EM. Overall, the cryo-EM reconstruction at 2.9 Å resolution is comparable to the best-resolved X-ray structure of the E. coli 70S ribosome (2.8 Å), but provides more detailed information (2.65 Å) at the functionally important ribosomal core. The cryo-EM map elucidates for the first time the structure of all 35 rRNA modifications in the bacterial ribosome, explaining their roles in fine-tuning ribosome structure and function and modulating the action of antibiotics. We also obtained atomic models for flexible parts of the ribosome such as ribosomal proteins L9 and L31. The refined cryo-EM-based model presents the currently most complete high-resolution structure of the E. coli ribosome, which demonstrates the power of cryo-EM in structure determination of large and dynamic macromolecular complexes. PubMed: 25707802DOI: 10.1038/nature14275 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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