3MCA

Structure of the Dom34-Hbs1 Complex and implications for its role in No-Go decay

Summary for 3MCA

• Entry DOI: 10.2210/pdb3mca/pdb
• Descriptor: Elongation factor 1 alpha-like protein, Protein dom34 (3 entities in total)
• Functional Keywords: protein protein complex, translation regulation, no-go decay, translation regulation-hydrolase complex, translation regulation/hydrolase
• Biological source: Schizosaccharomyces pombe (Fission yeast); More
• Cellular location: Cytoplasm: O74774 Q9USL5
• Total number of polymer chains: 2
• Total formula weight: 110495.68

Authors

Chen, L.,Song, H. (deposition date: 2010-03-28, release date: 2010-10-06, Last modification date: 2024-03-20)

Primary citation

Chen, L.,Muhlrad, D.,Hauryliuk, V.,Cheng, Z.,Lim, M.K.,Shyp, V.,Parker, R.,Song, H.
Structure of the Dom34-Hbs1 complex and implications for no-go decay
Nat.Struct.Mol.Biol., 17:1233-1240, 2010

PubMed Abstract: No-go decay (NGD) targets mRNAs with stalls in translation elongation for endonucleolytic cleavage in a process involving the Dom34 and Hbs1 proteins. The crystal structure of a Schizosaccharomyces pombe Dom34-Hbs1 complex reveals an overall shape similar to that of eRF1-eRF3-GTP and EF-Tu-tRNA-GDPNP. Similarly to eRF1 and GTP binding to eRF3, Dom34 and GTP bind to Hbs1 with strong cooperativity, and Dom34 acts as a GTP-dissociation inhibitor (GDI). A marked conformational change in Dom34 occurs upon binding to Hbs1, leading Dom34 to resemble a portion of a tRNA and to position a conserved basic region in a position expected to be near the peptidyl transferase center. These results support the idea that the Dom34-Hbs1 complex functions to terminate translation and thereby commit mRNAs to NGD. Consistent with this role, NGD at runs of arginine codons, which cause a strong block to elongation, is independent of the Dom34-Hbs1 complex.

PubMed: 20890290
DOI: 10.1038/nsmb.1922

Experimental method

X-RAY DIFFRACTION (2.74 Å)