2x7n

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Mechanism of eIF6s anti-association activity

Structural highlights

2x7n is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 11.8Å
Experimental data:Check to display Experimental Data
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RL23A_YEAST

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Mechanism of eIF6-mediated inhibition of ribosomal subunit joining.,Gartmann M, Blau M, Armache JP, Mielke T, Topf M, Beckmann R J Biol Chem. 2010 May 14;285(20):14848-51. Epub 2010 Mar 31. PMID:20356839[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Gartmann M, Blau M, Armache JP, Mielke T, Topf M, Beckmann R. Mechanism of eIF6-mediated inhibition of ribosomal subunit joining. J Biol Chem. 2010 May 14;285(20):14848-51. Epub 2010 Mar 31. PMID:20356839 doi:10.1074/jbc.C109.096057

Contents


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2x7n, resolution 11.80Å

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