Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Laure Yatime, Denmark
  • Yves Mechulam
  • ,
  • Sylvain Blanquet
  • ,
  • Emmanuelle Schmitt
  • Interdisciplinary Nanoscience Center
  • Department of Molecular Biology
Eukaryotic and archaeal initiation factors 2 (e/aIF2) are heterotrimeric proteins (alphabetagamma) supplying the small subunit of the ribosome with methionylated initiator tRNA. This study reports the crystallographic structure of an aIF2alphagamma heterodimer from Sulfolobus solfataricus bound to Gpp(NH)p-Mg(2+). aIF2gamma is in a closed conformation with the G domain packed on domains II and III. The C-terminal domain of aIF2alpha interacts with domain II of aIF2gamma. Conformations of the two switch regions involved in GTP binding are similar to those encountered in an EF1A:GTP:Phe-tRNA(Phe) complex. Comparison with the EF1A structure suggests that only the gamma subunit of the aIF2alphagamma heterodimer contacts tRNA. Because the alpha subunit markedly reinforces the affinity of tRNA for the gamma subunit, a contribution of the alpha subunit to the switch movements observed in the gamma structure is considered.
Original languageEnglish
JournalStructure
Volume14
Issue1
Pages (from-to)119-28
Number of pages10
ISSN0969-2126
DOIs
Publication statusPublished - 1 Jan 2006

    Research areas

  • Amino Acid Sequence, Archaeal Proteins, Binding Sites, Crystallography, X-Ray, Dimerization, Guanylyl Imidodiphosphate, Molecular Sequence Data, Peptide Initiation Factors, Protein Binding, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, RNA, Transfer, Met, Sulfolobus solfataricus

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