2iu1

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2iu1, resolution 1.80Å

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CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN

Overview

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.

About this Structure

2IU1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5., Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U, J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736

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