The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5

Christoph Bieniossek; Patrick Schütz; Mario Bumann; Andreas Limacher; Isabel Uson; Ulrich Baumann

doi:10.1016/j.jmb.2006.05.021

The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5

J Mol Biol. 2006 Jul 7;360(2):457-65. doi: 10.1016/j.jmb.2006.05.021. Epub 2006 May 24.

Authors

Christoph Bieniossek¹, Patrick Schütz, Mario Bumann, Andreas Limacher, Isabel Uson, Ulrich Baumann

Affiliation

¹ Departement für Chemie und Biochemie, Universität Bern, Freiestrasse 3, CH-3012 Bern, Switzerland.

PMID: 16781736
DOI: 10.1016/j.jmb.2006.05.021

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Binding Sites / genetics
Chromatography, Gel
Crystallography, X-Ray
Eukaryotic Initiation Factor-5 / chemistry*
Humans
Molecular Sequence Data
Mutation / genetics
Protein Structure, Tertiary
Sequence Alignment
Temperature

Substances

Eukaryotic Initiation Factor-5

Associated data

PDB/2IU1