2X7N
Mechanism of eIF6s anti-association activity
Summary for 2X7N
Entry DOI | 10.2210/pdb2x7n/pdb |
Related | 1G62 1K5Y 1S1I |
EMDB information | 1705 |
Descriptor | SARCIN-RICIN LOOP, EUKARYOTIC TRANSLATION INITIATION FACTOR 6, 60S RIBOSOMAL PROTEIN L23, ... (4 entities in total) |
Functional Keywords | ribosomal protein-rna complex, initiation factor, protein biosynthesis, ribosomal protein, ribonucleoprotein, ribosomal protein/rna |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
Total number of polymer chains | 4 |
Total formula weight | 53796.73 |
Authors | Gartmann, M.,Blau, M.,Armache, J.-P.,Mielke, T.,Topf, M.,Beckmann, R. (deposition date: 2010-03-02, release date: 2010-03-31, Last modification date: 2024-05-08) |
Primary citation | Gartmann, M.,Blau, M.,Armache, J.-P.,Mielke, T.,Topf, M.,Beckmann, R. Mechanism of Eif6-Mediated Inhibition of Ribosomal Subunit Joining. J.Biol.Chem., 285:14848-, 2010 Cited by PubMed Abstract: During the process of ribosomal assembly, the essential eukaryotic translation initiation factor 6 (eIF6) is known to act as a ribosomal anti-association factor. However, a molecular understanding of the anti-association activity of eIF6 is still missing. Here we present the cryo-electron microscopy reconstruction of a complex of the large ribosomal subunit with eukaryotic eIF6 from Saccharomyces cerevisiae. The structure reveals that the eIF6 binding site involves mainly rpL23 (L14p in Escherichia coli). Based on our structural data, we propose that the mechanism of the anti-association activity of eIF6 is based on steric hindrance of intersubunit bridge formation around the dynamic bridge B6. PubMed: 20356839DOI: 10.1074/JBC.C109.096057 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (11.8 Å) |
Structure validation
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