2IU1
Crystal structure of eIF5 C-terminal domain
Summary for 2IU1
| Entry DOI | 10.2210/pdb2iu1/pdb |
| Descriptor | EUKARYOTIC TRANSLATION INITIATION FACTOR 5 (2 entities in total) |
| Functional Keywords | mfc, eif5, gtp-binding, phosphorylation, protein biosynthesis, translation inititation, initiation factor, nucleotide-binding, transcription |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 24442.86 |
| Authors | Bieniossek, C.,Schuetz, P.,Baumann, U. (deposition date: 2006-05-26, release date: 2006-06-01, Last modification date: 2024-05-08) |
| Primary citation | Bieniossek, C.,Schutz, P.,Bumann, M.,Limacher, A.,Uson, I.,Baumann, U. The Crystal Structure of the Carboxy-Terminal Domain of Human Translation Initiation Factor Eif5. J.Mol.Biol., 360:457-, 2006 Cited by PubMed Abstract: 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. PubMed: 16781736DOI: 10.1016/J.JMB.2006.05.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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