| Literature DB >> 16781736 |
Christoph Bieniossek1, Patrick Schütz, Mario Bumann, Andreas Limacher, Isabel Uson, Ulrich Baumann.
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.Entities:
Mesh：
Substances：
Year: 2006 PMID： 16781736 DOI： 10.1016/j.jmb.2006.05.021
Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469