7R4X
Cryo-EM reconstruction of the human 40S ribosomal subunit - Full map
Summary for 7R4X
Entry DOI | 10.2210/pdb7r4x/pdb |
EMDB information | 14317 14318 14319 |
Descriptor | 60S ribosomal protein L41, 40S ribosomal protein S11, 40S ribosomal protein S15, ... (39 entities in total) |
Functional Keywords | ribosome, rrna modifications, post-translational modifications, cryo-em |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 35 |
Total formula weight | 1231506.53 |
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 citation | Pellegrino, 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: 36951107DOI: 10.1093/nar/gkad194 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.15 Å) |
Structure validation
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