AI Article Synopsis
- The translation initiation factor 2 (IF2) in eukaryotes and archaea helps deliver the initiator methionyl-tRNA to the small ribosomal subunit using GTP.
- Over the last two decades, significant research efforts have led to the crystallization of IF2 from the archaeon Sulfolobus solfataricus in ten different spatial arrangements.
- Analyzing these crystal structures provides insights into the functional mechanisms of the protein, particularly how certain molecular switches and nucleotide-binding elements contribute to its active and inactive states.
Article Abstract
Eukaryotic and archaeal translation initiation factor 2 in complex with GTP delivers the initiator methionyl-tRNA to the small ribosomal subunit. Over the past 20 years, thanks to the efforts of various research groups, including ours, this factor from the archaeon Sulfolobus solfataricus and its individual subunits have been crystallized in ten different space groups. Analysis of the molecular packing in these crystals makes it possible to better understand the roles of functionally significant switches and other elements of the nucleotide-binding pocket during the function of the factor as well as the influence of external effects on its transition between active and inactive states.
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| http://dx.doi.org/10.1107/S2059798324004029 | DOI Listing |
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