1rf8
|
Solution structure of the yeast translation initiation factor eIF4E in complex with m7GDP and eIF4GI residues 393 to 490
OverviewOverview
The eukaryotic initiation factor 4G (eIF4G) is the core of a multicomponent switch controlling gene expression at the level of translation initiation. It interacts with the small ribosomal subunit interacting protein, eIF3, and the eIF4E/cap-mRNA complex in order to load the ribosome onto mRNA during cap-dependent translation. We describe the solution structure of the complex between yeast eIF4E/cap and eIF4G (393-490). Binding triggers a coupled folding transition of eIF4G (393-490) and the eIF4E N terminus resulting in a molecular bracelet whereby eIF4G (393-490) forms a right-handed helical ring that wraps around the N terminus of eIF4E. Cofolding allosterically enhances association of eIF4E with the cap and is required for maintenance of optimal growth and polysome distributions in vivo. Our data explain how mRNA, eIF4E, and eIF4G exists as a stable mRNP that may facilitate multiple rounds of ribosomal loading during translation initiation, a key determinant in the overall rate of protein synthesis.
About this StructureAbout this Structure
1RF8 is a Protein complex structure of sequences from Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E., Gross JD, Moerke NJ, von der Haar T, Lugovskoy AA, Sachs AB, McCarthy JE, Wagner G, Cell. 2003 Dec 12;115(6):739-50. PMID:14675538
Page seeded by OCA on Thu Feb 21 14:50:13 2008