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PDBsum entry 2x7n

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protein dna_rna Protein-protein interface(s) links
Ribosomal protein/RNA PDB id
2x7n
Jmol
Contents
Protein chains
224 a.a. *
132 a.a. *
56 a.a. *
DNA/RNA
* Residue conservation analysis
PDB id:
2x7n
Name: Ribosomal protein/RNA
Title: Mechanism of eif6s anti-association activity
Structure: Sarcin-ricin loop. Chain: a. Fragment: 2684-2711. Eukaryotic translation initiation factor 6. Chain: b. Fragment: residues 1-224. Synonym: eif-6. 60s ribosomal protein l23. Chain: c.
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Organism_taxid: 4932
Authors: M.Gartmann,M.Blau,J.-P.Armache,T.Mielke,M.Topf,R.Beckmann
Key ref: M.Gartmann et al. (2010). Mechanism of eIF6-mediated inhibition of ribosomal subunit joining. J Biol Chem, 285, 14848-14851. PubMed id: 20356839 DOI: 10.1074/jbc.C109.096057
Date:
02-Mar-10     Release date:   31-Mar-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q12522  (IF6_YEAST) -  Eukaryotic translation initiation factor 6
Seq:
Struc:
245 a.a.
224 a.a.
Protein chain
Pfam   ArchSchema ?
P0CX41  (RL23A_YEAST) -  60S ribosomal protein L23-A
Seq:
Struc:
137 a.a.
132 a.a.
Protein chain
Pfam   ArchSchema ?
P04449  (RL24A_YEAST) -  60S ribosomal protein L24-A
Seq:
Struc:
155 a.a.
56 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     ribonucleoprotein complex   7 terms 
  Biological process     ribosome biogenesis   11 terms 
  Biochemical function     protein binding     5 terms  

 

 
DOI no: 10.1074/jbc.C109.096057 J Biol Chem 285:14848-14851 (2010)
PubMed id: 20356839  
 
 
Mechanism of eIF6-mediated inhibition of ribosomal subunit joining.
M.Gartmann, M.Blau, J.P.Armache, T.Mielke, M.Topf, R.Beckmann.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23142978 B.Bradatsch, C.Leidig, S.Granneman, M.Gnädig, D.Tollervey, B.Böttcher, R.Beckmann, and E.Hurt (2012).
Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel.
  Nat Struct Mol Biol, 19, 1234-1241.
PDB code: 3j2i
23142985 B.J.Greber, D.Boehringer, C.Montellese, and N.Ban (2012).
Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit.
  Nat Struct Mol Biol, 19, 1228-1233.
PDB codes: 4b6a 4b6b
21427765 A.Parsyan, Y.Svitkin, D.Shahbazian, C.Gkogkas, P.Lasko, W.C.Merrick, and N.Sonenberg (2011).
mRNA helicases: the tacticians of translational control.
  Nat Rev Mol Cell Biol, 12, 235-245.  
21448132 V.P.Pisareva, M.A.Skabkin, C.U.Hellen, T.V.Pestova, and A.V.Pisarev (2011).
Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes and stalled elongation complexes.
  EMBO J, 30, 1804-1817.  
20947765 C.J.Shoemaker, D.E.Eyler, and R.Green (2010).
Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay.
  Science, 330, 369-372.  
20670889 K.Y.Lo, Z.Li, C.Bussiere, S.Bresson, E.M.Marcotte, and A.W.Johnson (2010).
Defining the pathway of cytoplasmic maturation of the 60S ribosomal subunit.
  Mol Cell, 39, 196-208.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.