The Crystal Structure of the Carboxy-terminal Domain of Human Translation Initiation Factor Eif5.
From: Departement für Chemie und Biochemie, Universität Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.
Journal of molecular biology
- Publish Date: Jul 2006
- ISSN: 0022-2836
- Volume: 360
- Issue: 2
- Pages: 457-65
- Medium: Print
- Language: English
- Citation (JAMA): Bieniossek Christoph, Schütz Patrick, Bumann Mario, et al. The Crystal Structure of the Carboxy-terminal Domain of Human Translation Initiation Factor Eif5.. J. Mol. Biol. Jul 2006;360:457-65
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.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Chromatography, Gel, Crystallography, X-Ray, Eukaryotic Initiation Factor-5, Humans, Molecular Sequence Data, Mutation, Protein Structure, Tertiary, Sequence Alignment, Temperature
Check for Full Text / PubMed Unique Identifier (PMID): 16781736
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