Summary for 6Y57
Entry DOI | 10.2210/pdb6y57/pdb |
Related | 6Y0G 6Y2L |
EMDB information | 10668 10674 10690 |
Descriptor | mRNA, 60S ribosomal protein L5, 60S ribosomal protein L6, ... (85 entities in total) |
Functional Keywords | hybrid-pre state, ribosome |
Biological source | Homo sapiens More |
Total number of polymer chains | 82 |
Total formula weight | 3837443.72 |
Authors | Bhaskar, V.,Schenk, A.D.,Cavadini, S.,von Loeffelholz, O.,Natchiar, S.K.,Klaholz, B.P.,Chao, J.A. (deposition date: 2020-02-25, release date: 2020-04-15, Last modification date: 2024-05-22) |
Primary citation | Bhaskar, V.,Graff-Meyer, A.,Schenk, A.D.,Cavadini, S.,von Loeffelholz, O.,Natchiar, S.K.,Artus-Revel, C.G.,Hotz, H.R.,Bretones, G.,Klaholz, B.P.,Chao, J.A. Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes. Cell Rep, 31:107473-107473, 2020 Cited by PubMed Abstract: Ribosomes undergo multiple conformational transitions during translation elongation. Here, we report the high-resolution cryoelectron microscopy (cryo-EM) structure of the human 80S ribosome in the post-decoding pre-translocation state (classical-PRE) at 3.3-Å resolution along with the rotated (hybrid-PRE) and the post-translocation states (POST). The classical-PRE state ribosome structure reveals a previously unobserved interaction between the C-terminal region of the conserved ribosomal protein uS19 and the A- and P-site tRNAs and the mRNA in the decoding site. In addition to changes in the inter-subunit bridges, analysis of different ribosomal conformations reveals the dynamic nature of this domain and suggests a role in tRNA accommodation and translocation during elongation. Furthermore, we show that disease-associated mutations in uS19 result in increased frameshifting. Together, this structure-function analysis provides mechanistic insights into the role of the uS19 C-terminal tail in the context of mammalian ribosomes. PubMed: 32268098DOI: 10.1016/j.celrep.2020.03.037 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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