Crystal-packing analysis of translation initiation factor 2 reveals new details of its function

Acta Crystallogr D Struct Biol. 2024 Jul 1;80(Pt 7):464-473. doi: 10.1107/S2059798324004029. Epub 2024 Jun 7.

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.

Keywords: G-domain; molecular packing; ribosomal GTPases; translation initiation; translation initiation factor 2.

MeSH terms

  • Archaeal Proteins* / chemistry
  • Archaeal Proteins* / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Guanosine Triphosphate / chemistry
  • Guanosine Triphosphate / metabolism
  • Models, Molecular
  • Peptide Initiation Factors / chemistry
  • Peptide Initiation Factors / metabolism
  • Protein Conformation
  • RNA, Transfer, Met / chemistry
  • RNA, Transfer, Met / metabolism
  • Sulfolobus solfataricus* / chemistry
  • Sulfolobus solfataricus* / metabolism

Substances

  • Archaeal Proteins
  • Guanosine Triphosphate
  • Peptide Initiation Factors
  • initiation factor 2, archaeal
  • RNA, Transfer, Met