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7K00

Structure of the Bacterial Ribosome at 2 Angstrom Resolution

This is a non-PDB format compatible entry.
Summary for 7K00
Entry DOI10.2210/pdb7k00/pdb
EMDB information22586
Descriptor16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (62 entities in total)
Functional Keywordsantibiotics, post-translational modifications, post-transcriptional modifications, ribosome
Biological sourceEscherichia coli
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Total number of polymer chains56
Total formula weight2209971.59
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 citationWatson, 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: 32924932
DOI: 10.7554/eLife.60482
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.98 Å)
Structure validation

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