PDBsum entry 2iu1

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protein links
Transcription PDB id
Protein chain
179 a.a. *
Waters ×139
* Residue conservation analysis
PDB id:
Name: Transcription
Title: Crystal structure of eif5 c-terminal domain
Structure: Eukaryotic translation initiation factor 5. Chain: a. Fragment: c-terminal domain residues 232-431. Synonym: eif5. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008.
1.80Å     R-factor:   0.188     R-free:   0.221
Authors: C.Bieniossek,P.Schuetz,U.Baumann
Key ref:
C.Bieniossek et al. (2006). The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J Mol Biol, 360, 457-465. PubMed id: 16781736 DOI: 10.1016/j.jmb.2006.05.021
26-May-06     Release date:   01-Jun-06    
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Protein chain
Pfam   ArchSchema ?
P55010  (IF5_HUMAN) -  Eukaryotic translation initiation factor 5
431 a.a.
179 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)


DOI no: 10.1016/j.jmb.2006.05.021 J Mol Biol 360:457-465 (2006)
PubMed id: 16781736  
The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5.
C.Bieniossek, P.Schütz, M.Bumann, A.Limacher, I.Uson, U.Baumann.
The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively.
  Selected figure(s)  
Figure 3.
Figure 3. Top: Cartoon representation of eIF5-CTD. Shown is a cartoon in rainbow coloring (N-terminus blue, C-terminus red). AA-box 1 (AA1) and AA-box 2 (AA2) are shown in grey and magenta, respectively. Bottom: Stereo cartoon overlay eIF5-CTD and eIF2B-ε. Shown is an overlay of eIF5-CTD (rainbow-colored, blue (N-terminus) to red (C-terminus) and eIF2B-ε (grey, PDB code 1PAQ). The figure was generated with PYMOL (
Figure 5.
Figure 5. Mapping of temperature-sensitive mutations. Shown is a stereo trace as in Figure 4(a) (top) with the relevant residues (Leu270, Leu284, Phe285, Ile293, Leu314, Leu337, Met340, Trp354) shown as sticks.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2006, 360, 457-465) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19684596 D.D.Rodríguez, C.Grosse, S.Himmel, C.González, Ilarduya, S.Becker, G.M.Sheldrick, and I.Usón (2009).
Crystallographic ab initio protein structure solution below atomic resolution.
  Nat Methods, 6, 651-653.
PDB code: 3gwh
17974565 M.Reibarkh, Y.Yamamoto, C.R.Singh, F.del Rio, A.Fahmy, B.Lee, R.E.Luna, M.Ii, G.Wagner, and K.Asano (2008).
Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection.
  J Biol Chem, 283, 1094-1103.
PDB code: 2ogh
17526738 S.S.Mohammad-Qureshi, R.Haddad, E.J.Hemingway, J.P.Richardson, and G.D.Pavitt (2007).
Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange.
  Mol Cell Biol, 27, 5225-5234.  
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