6Y2L

Structure of human ribosome in POST state

This is a non-PDB format compatible entry.

Summary for 6Y2L

• Entry DOI: 10.2210/pdb6y2l/pdb
• Related: 6Y0G
• EMDB information: 10668 10674
• Descriptor: mRNA, 60S ribosomal protein L5, 60S ribosomal protein L6, ... (84 entities in total)
• Functional Keywords: post state, cycloheximide, ribosome
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 80
• Total formula weight: 3785614.81

Authors

Bhaskar, V.,Schenk, A.D.,Cavadini, S.,von Loeffelholz, O.,Natchiar, S.K.,Klaholz, B.P.,Chao, J.A. (deposition date: 2020-02-16, 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

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: 32268098
DOI: 10.1016/j.celrep.2020.03.037

Experimental method

ELECTRON MICROSCOPY (3 Å)