5LZT

Structure of the mammalian ribosomal termination complex with eRF1 and eRF3.

This is a non-PDB format compatible entry.

Summary for 5LZT

• Entry DOI: 10.2210/pdb5lzt/pdb
• EMDB information: 4131
• Descriptor: uL2, uL5, eL13, ... (90 entities in total)
• Functional Keywords: translation, elongation, ribosome
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 87
• Total formula weight: 3544784.82

Authors

Shao, S.,Murray, J.,Brown, A.,Taunton, J.,Ramakrishnan, V.,Hegde, R.S. (deposition date: 2016-10-02, release date: 2016-11-30, Last modification date: 2019-12-11)

Primary citation

Shao, S.,Murray, J.,Brown, A.,Taunton, J.,Ramakrishnan, V.,Hegde, R.S.
Decoding Mammalian Ribosome-mRNA States by Translational GTPase Complexes.
Cell, 167:1229-1240.e15, 2016

PubMed Abstract: In eukaryotes, accurate protein synthesis relies on a family of translational GTPases that pair with specific decoding factors to decipher the mRNA code on ribosomes. We present structures of the mammalian ribosome engaged with decoding factor⋅GTPase complexes representing intermediates of translation elongation (aminoacyl-tRNA⋅eEF1A), termination (eRF1⋅eRF3), and ribosome rescue (Pelota⋅Hbs1l). Comparative analyses reveal that each decoding factor exploits the plasticity of the ribosomal decoding center to differentially remodel ribosomal proteins and rRNA. This leads to varying degrees of large-scale ribosome movements and implies distinct mechanisms for communicating information from the decoding center to each GTPase. Additional structural snapshots of the translation termination pathway reveal the conformational changes that choreograph the accommodation of decoding factors into the peptidyl transferase center. Our results provide a structural framework for how different states of the mammalian ribosome are selectively recognized by the appropriate decoding factor⋅GTPase complex to ensure translational fidelity.

PubMed: 27863242
DOI: 10.1016/j.cell.2016.10.046

Experimental method

ELECTRON MICROSCOPY (3.65 Å)