3J5Y
Structure of the mammalian ribosomal pre-termination complex associated with eRF1-eRF3-GDPNP
Replaces: 3J2KSummary for 3J5Y
Entry DOI | 10.2210/pdb3j5y/pdb |
EMDB information | 5801 |
Descriptor | Eukaryotic 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 Keywords | translation termination, erf1, erf3, trnaleu, ribosome, mammalian, translation-rna complex, translation/rna |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 126079.50 |
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 citation | des 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: 24335085DOI: 10.1093/nar/gkt1279 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (9.7 Å) |
Structure validation
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