3IZQ

Structure of the Dom34-Hbs1-GDPNP complex bound to a translating ribosome

Summary for 3IZQ

• Entry DOI: 10.2210/pdb3izq/pdb
• EMDB information: 1811
• Descriptor: Protein DOM34, Elongation factor 1 alpha-like protein (2 entities in total)
• Functional Keywords: no-go mrna decay, ribosomal protein, hydrolase
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Total number of polymer chains: 2
• Total formula weight: 112946.20

Authors

Becker, T.,Armache, J.-P.,Jarasch, A.,Anger, A.M.,Villa, E.,Sieber, H.,Abdel Motaal, B.,Mielke, T.,Berninghausen, O.,Beckmann, R. (deposition date: 2010-11-30, release date: 2011-06-01, Last modification date: 2024-02-21)

Primary citation

Becker, T.,Armache, J.P.,Jarasch, A.,Anger, A.M.,Villa, E.,Sieber, H.,Motaal, B.A.,Mielke, T.,Berninghausen, O.,Beckmann, R.
Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome.
Nat.Struct.Mol.Biol., 18:715-720, 2011

PubMed Abstract: No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the docking of crystal structures and homology models. Moreover, the close structural similarity of Dom34 and Hbs1 to eukaryotic release factors (eRFs) enabled us to propose a model for the ribosome-bound eRF1-eRF3 complex. Collectively, our data provide structural insights into how stalled mRNA is recognized on the ribosome and how the eRF complex can simultaneously recognize stop codons and catalyze peptide release.

PubMed: 21623367
DOI: 10.1038/nsmb.2057

Experimental method

ELECTRON MICROSCOPY (9.5 Å)