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PDBsum entry 3agj

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protein ligands metals Protein-protein interface(s) links
Translation/hydrolase PDB id
3agj
Jmol
Contents
Protein chains
432 a.a. *
357 a.a. *
Ligands
GTP ×4
Metals
_MG ×4
Waters ×1349
* Residue conservation analysis
PDB id:
3agj
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.
Resolution:
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
Date:
01-Apr-10     Release date:   06-Oct-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

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

 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.
 
  ABSTRACT  
 
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
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 codes are shown on the right.