Structure and Function of Archaeal Translation Initiation Factor 2 Fragments Containing Cys2-Cys2 Motifs

Biochemistry (Mosc). 2021 Aug;86(8):1003-1011. doi: 10.1134/S0006297921080101.

Abstract

The heterotrimeric (αβγ) translation initiation factor 2 of archaea and eukaryotes (a/eIF2) supplies the P-site of the ribosome with the initiation tRNA. Its two subunits (β and γ) contain the Cys2-Cys2 motif, which is capable of forming a stable zinc finger structure in the presence of zinc ions. In this work, comparative analysis of the fragments containing Cys2-Cys2 motifs in the aIF2β and aIF2γ structures from different organisms was carried out and their environments in crystals was analyzed. Based on the obtained data, a conclusion was made that the conformation and role of these fragments in the β- and γ-subunits of the aIF2 are different.

Keywords: Cys2-Cys2 motif; Sulfolobus solfataricus; crystal structure; translation initiation factor 2; zinc finger.

MeSH terms

  • Archaeal Proteins / chemistry*
  • Binding Sites
  • Crystallography, X-Ray
  • Cysteine / chemistry*
  • Humans
  • Ions
  • Molecular Conformation
  • Peptide Initiation Factors / chemistry*
  • Prokaryotic Initiation Factor-2 / chemistry*
  • Protein Conformation
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Subunits / chemistry
  • Sulfolobus solfataricus / chemistry
  • Zinc
  • Zinc Fingers

Substances

  • Archaeal Proteins
  • Ions
  • Peptide Initiation Factors
  • Prokaryotic Initiation Factor-2
  • Protein Subunits
  • initiation factor 2, archaeal
  • Zinc
  • Cysteine