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1kl9

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Image:1kl9.jpg

1kl9, resolution 1.90Å

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Crystal structure of the N-terminal segment of Human eukaryotic initiation factor 2alpha

Contents

Overview

Eukaryotic translation initiation factor 2alpha (eIF2alpha) is a member of, the eIF2 heterotrimeric complex that binds and delivers Met-tRNA(i)(Met), to the 40 S ribosomal subunit in a GTP-dependent manner., Phosphorylation/dephosphorylation of eIF2alpha at Ser-51 is the major, regulator of protein synthesis in eukaryotic cells. Here, we report the, first structural analysis on eIF2, the three-dimensional structure of a, 22-kDa N-terminal portion of human eIF2alpha by x-ray diffraction at 1.9 A, resolution. This structure contains two major domains. The N terminus is a, beta-barrel with five antiparallel beta-strands in an oligonucleotide, binding domain (OB domain) fold. The phosphorylation site (Ser-51) is on, the loop connecting beta3 and beta4 in the OB domain. A helical domain, follows the OB domain, and the first helix has extensive interactions, including a disulfide bridge, to fix its orientation with respect to the, OB domain. The two domains meet along a negatively charged groove with, highly conserved residues, indicating a likely site for protein-protein, interaction.

Disease

Known disease associated with this structure: Wolcott-Rallison syndrome OMIM:[604032]

About this Structure

1KL9 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha., Nonato MC, Widom J, Clardy J, J Biol Chem. 2002 May 10;277(19):17057-61. Epub 2002 Feb 21. PMID:11859078

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