7K00
Structure of the Bacterial Ribosome at 2 Angstrom Resolution
This is a non-PDB format compatible entry.
Summary for 7K00
Entry DOI | 10.2210/pdb7k00/pdb |
EMDB information | 22586 |
Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (62 entities in total) |
Functional Keywords | antibiotics, post-translational modifications, post-transcriptional modifications, ribosome |
Biological source | Escherichia coli More |
Total number of polymer chains | 56 |
Total formula weight | 2209971.59 |
Authors | Watson, Z.L.,Ward, F.R.,Meheust, R.,Ad, O.,Schepartz, A.,Banfield, J.F.,Cate, J.H.D. (deposition date: 2020-09-02, release date: 2020-09-23, Last modification date: 2025-03-19) |
Primary citation | Watson, Z.L.,Ward, F.R.,Meheust, R.,Ad, O.,Schepartz, A.,Banfield, J.F.,Cate, J.H. Structure of the bacterial ribosome at 2 angstrom resolution. Elife, 9:-, 2020 Cited by PubMed Abstract: Using cryo-electron microscopy (cryo-EM), we determined the structure of the 70S ribosome with a global resolution of 2.0 Å. The maps reveal unambiguous positioning of protein and RNA residues, their detailed chemical interactions, and chemical modifications. Notable features include the first examples of isopeptide and thioamide backbone substitutions in ribosomal proteins, the former likely conserved in all domains of life. The maps also reveal extensive solvation of the small (30S) ribosomal subunit, and interactions with A-site and P-site tRNAs, mRNA, and the antibiotic paromomycin. The maps and models of the bacterial ribosome presented here now allow a deeper phylogenetic analysis of ribosomal components including structural conservation to the level of solvation. The high quality of the maps should enable future structural analyses of the chemical basis for translation and aid the development of robust tools for cryo-EM structure modeling and refinement. PubMed: 32924932DOI: 10.7554/eLife.60482 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (1.98 Å) |
Structure validation
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