Superposition of a tRNASer acceptor stem microhelix into the seryl-tRNA synthetase complex

Biochem Biophys Res Commun. 2007 Oct 19;362(2):415-8. doi: 10.1016/j.bbrc.2007.07.178. Epub 2007 Aug 10.

Abstract

Aminoacyl-tRNA synthetases catalyze the formation of aminoacyl-tRNAs. Seryl-tRNA synthetase is a class II synthetase, which depends on rather few and simple identity elements in tRNA(Ser) to determine the amino acid specificity. tRNA(Ser) acceptor stem microhelices can be aminoacylated with serine, which makes this part of the tRNA a valuable tool for investigating the structural motifs in a tRNA(Ser)-seryl-tRNA synthetase complex. A 1.8A-resolution tRNA(Ser) acceptor stem crystal structure was superimposed to a 2.9A-resolution crystal structure of a tRNA(Ser)-seryl-tRNA synthetase complex for a visualization of the binding environment of the tRNA(Ser) microhelix.

MeSH terms

  • Anticodon / chemistry
  • Anticodon / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Binding
  • RNA, Transfer, Amino Acyl / chemistry
  • RNA, Transfer, Amino Acyl / metabolism
  • RNA, Transfer, Ser / chemistry*
  • RNA, Transfer, Ser / metabolism
  • Serine-tRNA Ligase / chemistry*
  • Serine-tRNA Ligase / metabolism

Substances

  • Anticodon
  • RNA, Transfer, Amino Acyl
  • RNA, Transfer, Ser
  • Serine-tRNA Ligase