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2X7N

Mechanism of eIF6s anti-association activity

Summary for 2X7N
Entry DOI10.2210/pdb2x7n/pdb
Related1G62 1K5Y 1S1I
EMDB information1705
DescriptorSARCIN-RICIN LOOP, EUKARYOTIC TRANSLATION INITIATION FACTOR 6, 60S RIBOSOMAL PROTEIN L23, ... (4 entities in total)
Functional Keywordsribosomal protein-rna complex, initiation factor, protein biosynthesis, ribosomal protein, ribonucleoprotein, ribosomal protein/rna
Biological sourceSACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
More
Total number of polymer chains4
Total formula weight53796.73
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 citationGartmann, 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: 20356839
DOI: 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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