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The crystal structure of the γ-subunit of translation initiation factor 2 from the archaeon Sulfolobus solfataricus (SsoIF2γ) has been solved based on perfectly hemihedral twinned data. The protein was cocrystallized with the 10-fold molar excess of GTP analog (GDPCP) over protein. However, no nucleotide was found in the structure, and the model demonstrated the apo form of the protein. Two slightly...
Archaeal translation initiation factor 2 (aIF2) is homologous to its eukaryotic counterpart (eIF2). It is a heterotrimeric protein consisting of α, β, and γ subunits. The protein e/aIF2 forms a ternary complex with guanosine 5′-triphosphate and the initiator methionyl-tRNA (Met-tRNAi) and delivers the latter to the ribosome. In archaea, translation initiation factor 2 has an additional function. The...
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