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TitleStructure of the mammalian ribosomal pre-termination complex associated with eRF1.eRF3.GDPNP.
Journal, issue, pagesNucleic Acids Res, Vol. 42, Issue 5, Page 3409-3418, Year 2014
Publish dateDec 11, 2013
AuthorsAmédée des Georges / Yaser Hashem / Anett Unbehaun / Robert A Grassucci / Derek Taylor / Christopher U T Hellen / Tatyana V Pestova / Joachim Frank /
PubMed AbstractEukaryotic 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- ...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.
External linksNucleic Acids Res / PubMed:24335085 / PubMed Central
MethodsEM (single particle)
Resolution9.7 Å
Structure data

5801

3j5y

EMDB-5801, PDB-3j5y:
Structure of the mammalian ribosomal pre-termination complex associated with eRF1-eRF3-GDPNP
Method: EM (single particle) / Resolution: 9.7 Å

Source
  • oryctolagus cuniculus (rabbit)
  • homo sapiens (human)
KeywordsTRANSLATION/RNA / Translation termination / eRF1 / eRF3 / tRNAleu / ribosome / mammalian / TRANSLATION-RNA complex

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