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8B0X

Translating 70S ribosome in the unrotated state (P and E, tRNAs)

This is a non-PDB format compatible entry.
Summary for 8B0X
Entry DOI10.2210/pdb8b0x/pdb
EMDB information15793 15794 15795 15796 15797
Descriptor50S ribosomal protein L33, 30S ribosomal protein S6, 30S ribosomal protein S7, ... (57 entities in total)
Functional Keywords70s, bacterial, translation, high-resolution, ribosome
Biological sourceEscherichia coli B
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Total number of polymer chains53
Total formula weight2185216.17
Authors
Fromm, S.A.,O'Connor, K.M.,Purdy, M.,Bhatt, P.R.,Loughran, G.,Atkins, J.F.,Jomaa, A.,Mattei, S. (deposition date: 2022-09-08, release date: 2022-11-30, Last modification date: 2025-04-16)
Primary citationFromm, S.A.,O'Connor, K.M.,Purdy, M.,Bhatt, P.R.,Loughran, G.,Atkins, J.F.,Jomaa, A.,Mattei, S.
The translating bacterial ribosome at 1.55 angstrom resolution generated by cryo-EM imaging services.
Nat Commun, 14:1095-1095, 2023
Cited by
PubMed Abstract: Our understanding of protein synthesis has been conceptualised around the structure and function of the bacterial ribosome. This complex macromolecular machine is the target of important antimicrobial drugs, an integral line of defence against infectious diseases. Here, we describe how open access to cryo-electron microscopy facilities combined with bespoke user support enabled structural determination of the translating ribosome from Escherichia coli at 1.55 Å resolution. The obtained structures allow for direct determination of the rRNA sequence to identify ribosome polymorphism sites in the E. coli strain used in this study and enable interpretation of the ribosomal active and peripheral sites at unprecedented resolution. This includes scarcely populated chimeric hybrid states of the ribosome engaged in several tRNA translocation steps resolved at ~2 Å resolution. The current map not only improves our understanding of protein synthesis but also allows for more precise structure-based drug design of antibiotics to tackle rising bacterial resistance.
PubMed: 36841832
DOI: 10.1038/s41467-023-36742-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.55 Å)
Structure validation

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