5YT0
Crystal structure of the complex of archaeal ribosomal stalk protein aP1 and archaeal translation initiation factor aIF5B
Summary for 5YT0
| Entry DOI | 10.2210/pdb5yt0/pdb |
| Related | 5FG3 |
| Descriptor | Probable translation initiation factor IF-2, Archaeal ribosomal stalk protein aP1, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | translation initiation factor, ribosomal stalk protein, complex, translation |
| Biological source | Aeropyrum pernix K1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 43153.90 |
| Authors | Murakami, R.,Singh, C.R.,Morris, J.,Tang, L.,Harmon, I.,Miyoshi, T.,Ito, K.,Asano, K.,Uchiumi, T. (deposition date: 2017-11-16, release date: 2018-06-27, Last modification date: 2024-03-27) |
| Primary citation | Murakami, R.,Singh, C.R.,Morris, J.,Tang, L.,Harmon, I.,Takasu, A.,Miyoshi, T.,Ito, K.,Asano, K.,Uchiumi, T. The Interaction between the Ribosomal Stalk Proteins and Translation Initiation Factor 5B Promotes Translation Initiation Mol. Cell. Biol., 38:-, 2018 Cited by PubMed Abstract: Ribosomal stalk proteins recruit translation elongation GTPases to the factor-binding center of the ribosome. Initiation factor 5B (eIF5B in eukaryotes and aIF5B in archaea) is a universally conserved GTPase that promotes the joining of the large and small ribosomal subunits during translation initiation. Here we show that aIF5B binds to the C-terminal tail of the stalk protein. In the cocrystal structure, the interaction occurs between the hydrophobic amino acids of the stalk C-terminal tail and a small hydrophobic pocket on the surface of the GTP-binding domain (domain I) of aIF5B. A substitution mutation altering the hydrophobic pocket of yeast eIF5B resulted in a marked reduction in ribosome-dependent eIF5B GTPase activity In yeast cells, the eIF5B mutation affected growth and impaired expression during amino acid starvation via a defect in start site selection for the first upstream open reading frame in mRNA, as observed with the eIF5B deletion mutant. The deletion of two of the four stalk proteins diminished polyribosome levels (indicating defective translation initiation) and starvation-induced expression, both of which were suppressible by eIF5B overexpression. Thus, the mutual interaction between a/eIF5B and the ribosomal stalk plays an important role in subunit joining during translation initiation . PubMed: 29844065DOI: 10.1128/MCB.00067-18 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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