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7R4X

Cryo-EM reconstruction of the human 40S ribosomal subunit - Full map

Summary for 7R4X
Entry DOI10.2210/pdb7r4x/pdb
EMDB information14317 14318 14319
Descriptor60S ribosomal protein L41, 40S ribosomal protein S11, 40S ribosomal protein S15, ... (39 entities in total)
Functional Keywordsribosome, rrna modifications, post-translational modifications, cryo-em
Biological sourceHomo sapiens (human)
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Total number of polymer chains35
Total formula weight1231506.53
Authors
Pellegrino, S.,Dent, K.C.,Spikes, T.,Warren, A.J. (deposition date: 2022-02-09, release date: 2023-02-22, Last modification date: 2024-04-24)
Primary citationPellegrino, S.,Dent, K.C.,Spikes, T.,Warren, A.J.
Cryo-EM reconstruction of the human 40S ribosomal subunit at 2.15 angstrom resolution.
Nucleic Acids Res., 51:4043-4054, 2023
Cited by
PubMed Abstract: The chemical modification of ribosomal RNA and proteins is critical for ribosome assembly, for protein synthesis and may drive ribosome specialisation in development and disease. However, the inability to accurately visualise these modifications has limited mechanistic understanding of the role of these modifications in ribosome function. Here we report the 2.15 Å resolution cryo-EM reconstruction of the human 40S ribosomal subunit. We directly visualise post-transcriptional modifications within the 18S rRNA and four post-translational modifications of ribosomal proteins. Additionally, we interpret the solvation shells in the core regions of the 40S ribosomal subunit and reveal how potassium and magnesium ions establish both universally conserved and eukaryote-specific coordination to promote the stabilisation and folding of key ribosomal elements. This work provides unprecedented structural details for the human 40S ribosomal subunit that will serve as an important reference for unravelling the functional role of ribosomal RNA modifications.
PubMed: 36951107
DOI: 10.1093/nar/gkad194
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.15 Å)
Structure validation

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