1KL9

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

Summary for 1KL9

• Entry DOI: 10.2210/pdb1kl9/pdb
• Descriptor: EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1, ZINC ION (3 entities in total)
• Functional Keywords: ob fold, helical domain, translation
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, Stress granule : P05198
• Total number of polymer chains: 1
• Total formula weight: 21700.70

Authors

Nonato, M.C.,Widom, J.,Clardy, J. (deposition date: 2001-12-11, release date: 2002-03-11, Last modification date: 2024-10-16)

Primary citation

Nonato, M.C.,Widom, J.,Clardy, J.
Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha
J.Biol.Chem., 277:17057-17061, 2002

PubMed Abstract: 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.

PubMed: 11859078
DOI: 10.1074/jbc.M111804200

Experimental method

X-RAY DIFFRACTION (1.9 Å)