PDBsum entry 3agj

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protein ligands metals Protein-protein interface(s) links
Translation/hydrolase PDB id
Protein chains
432 a.a. *
357 a.a. *
GTP ×4
_MG ×4
Waters ×1349
* Residue conservation analysis
Superseded by: 3wxm
PDB id:
Name: Translation/hydrolase
Title: Crystal structure of archaeal pelota and gtp-bound ef1 alpha
Structure: Elongation factor 1-alpha. Chain: a, c, e, g. Synonym: ef-1-alpha, elongation factor tu, ef-tu. Engineered: yes. Protein pelota homolog. Chain: b, d, f, h. Engineered: yes
Source: Aeropyrum pernix. Organism_taxid: 56636. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.30Å     R-factor:   0.210     R-free:   0.265
Authors: K.Kobayashi,I.Kikuno,R.Ishitani,K.Ito,O.Nureki
Key ref: K.Kobayashi et al. (2010). Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex. Proc Natl Acad Sci U S A, 107, 17575-17579. PubMed id: 20876129
01-Apr-10     Release date:   06-Oct-10    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9YAV0  (EF1A_AERPE) -  Elongation factor 1-alpha
437 a.a.
432 a.a.
Protein chains
Pfam   ArchSchema ?
Q9YAZ5  (PELO_AERPE) -  Protein pelota homolog
356 a.a.
357 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains B, D, F, H: E.C.3.1.-.-
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     nuclear-transcribed mRNA catabolic process, no-go decay   7 terms 
  Biochemical function     nucleotide binding     8 terms  


Proc Natl Acad Sci U S A 107:17575-17579 (2010)
PubMed id: 20876129  
Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex.
K.Kobayashi, I.Kikuno, K.Kuroha, K.Saito, K.Ito, R.Ishitani, T.Inada, O.Nureki.
No abstract given.


Literature references that cite this PDB file's key reference

  PubMed id Reference
22664987 C.J.Shoemaker, and R.Green (2012).
Translation drives mRNA quality control.
  Nat Struct Mol Biol, 19, 594-601.  
23072885 M.Graille, and B.Séraphin (2012).
Surveillance pathways rescuing eukaryotic ribosomes lost in translation.
  Nat Rev Mol Cell Biol, 13, 727-735.  
22358840 T.Becker, S.Franckenberg, S.Wickles, C.J.Shoemaker, A.M.Anger, J.P.Armache, H.Sieber, C.Ungewickell, O.Berninghausen, I.Daberkow, A.Karcher, M.Thomm, K.P.Hopfner, R.Green, and R.Beckmann (2012).
Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.
  Nature, 482, 501-506.
PDB codes: 3j15 3j16
21623367 T.Becker, J.P.Armache, A.Jarasch, A.M.Anger, E.Villa, H.Sieber, B.A.Motaal, T.Mielke, O.Berninghausen, and R.Beckmann (2011).
Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome.
  Nat Struct Mol Biol, 18, 715-720.
PDB code: 3izq
21102444 A.M.van den Elzen, J.Henri, N.Lazar, M.E.Gas, D.Durand, F.Lacroute, M.Nicaise, H.van Tilbeurgh, B.Séraphin, and M.Graille (2010).
Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.
  Nat Struct Mol Biol, 17, 1446-1452.
PDB codes: 3p26 3p27
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