Structural highlights
FunctionEIF2A_SCHPO Functions in the early steps of protein synthesis of a small number of specific mRNAs. Acts by directing the binding of methionyl-tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it binds methionyl-tRNAi to 40 S subunits in a codon-dependent manner, whereas the eIF-2 complex binds methionyl-tRNAi to 40 S subunits in a GTP-dependent manner. May act by impiging the expression of specific proteins (By similarity). Publication Abstract from PubMedThe eukaryotic translation initiation factor 2A (eIF2A) was identified as a factor that stimulates the binding of methionylated initiator tRNA (Met-tRNA i Met ) to the 40S ribosomal subunit, but its physiological role remains poorly defined. Recently, eIF2A was shown to be involved in unconventional translation initiation from CUG codons and in viral protein synthesis under stress conditions where eIF2 is inactivated. We determined the crystal structure of the WD-repeat domain of Schizosaccharomyces pombe eIF2A at 2.5 A resolution. The structure adopts a novel nine-bladed beta-propeller fold. In contrast to the usual beta-propeller proteins, the central channel of the molecule has the narrower opening on the bottom of the protein and the wider opening on the top. Highly conserved residues are concentrated in the positively-charged top face, suggesting the importance of this face for interactions with nucleic acids or other initiation factors. Crystal structure of the eukaryotic translation initiation factor 2A from Schizosaccharomyces pombe.,Kashiwagi K, Ito T, Yokoyama S J Struct Funct Genomics. 2014 Feb 26. PMID:24569939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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