Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3J5Y

Structure of the mammalian ribosomal pre-termination complex associated with eRF1-eRF3-GDPNP

Replaces:  3J2K
Summary for 3J5Y
Entry DOI10.2210/pdb3j5y/pdb
EMDB information5801
DescriptorEukaryotic peptide chain release factor subunit 1, Eukaryotic peptide chain release factor GTP-binding subunit ERF3A, 5'-R(*AP*UP*UP*GP*UP*AP*AP*AP*AP*A)-3', ... (4 entities in total)
Functional Keywordstranslation termination, erf1, erf3, trnaleu, ribosome, mammalian, translation-rna complex, translation/rna
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight126079.50
Authors
des Georges, A.,Hashem, Y.,Unbehaun, A.,Grassucci, R.A.,Taylor, D.,Hellen, C.U.T.,Pestova, T.V.,Frank, J. (deposition date: 2013-11-21, release date: 2013-12-25, Last modification date: 2024-11-06)
Primary citationdes Georges, A.,Hashem, Y.,Unbehaun, A.,Grassucci, R.A.,Taylor, D.,Hellen, C.U.,Pestova, T.V.,Frank, J.
Structure of the mammalian ribosomal pre-termination complex associated with eRF1*eRF3*GDPNP.
Nucleic Acids Res., 42:3409-3418, 2014
Cited by
PubMed Abstract: Eukaryotic translation termination results from the complex functional interplay between two release factors, eRF1 and eRF3, in which GTP hydrolysis by eRF3 couples codon recognition with peptidyl-tRNA hydrolysis by eRF1. Here, we present a cryo-electron microscopy structure of pre-termination complexes associated with eRF1•eRF3•GDPNP at 9.7 -Å resolution, which corresponds to the initial pre-GTP hydrolysis stage of factor attachment and stop codon recognition. It reveals the ribosomal positions of eRFs and provides insights into the mechanisms of stop codon recognition and triggering of eRF3's GTPase activity.
PubMed: 24335085
DOI: 10.1093/nar/gkt1279
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (9.7 Å)
Structure validation

237992

数据于2025-06-25公开中

PDB statisticsPDBj update infoContact PDBjnumon