Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome

J Mol Biol. 2016 Sep 11;428(18):3570-3576. doi: 10.1016/j.jmb.2016.05.011. Epub 2016 May 16.

Abstract

Eukaryotic translation initiation factor eIF5A promotes protein synthesis by resolving polyproline-induced ribosomal stalling. Here, we report a 3.25-Å resolution crystal structure of eIF5A bound to the yeast 80S ribosome. The structure reveals a previously unseen conformation of an eIF5A-ribosome complex and highlights a possible functional link between conformational changes of the ribosome during protein synthesis and the eIF5A-ribosome association.

Keywords: crystallography; eIF5A; hypusine; ribosome; structure.

MeSH terms

  • Crystallography, X-Ray
  • Eukaryotic Translation Initiation Factor 5A
  • Models, Molecular
  • Peptide Initiation Factors / chemistry*
  • Peptide Initiation Factors / metabolism*
  • Protein Binding
  • Protein Biosynthesis
  • Protein Conformation
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism*
  • Ribosomes / chemistry*
  • Ribosomes / metabolism*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / enzymology

Substances

  • Peptide Initiation Factors
  • RNA-Binding Proteins