How can elongation factors EF-G and EF-Tu discriminate the functional state of the ribosome using the same binding site?

FEBS Lett. 2005 Oct 24;579(25):5439-42. doi: 10.1016/j.febslet.2005.09.010. Epub 2005 Sep 26.

Abstract

Elongation factors EF-G and EF-Tu are structural homologues and share near-identical binding sites on the ribosome, which encompass the GTPase-associated centre (GAC) and the sarcin-ricin loop (SRL). The SRL is fixed structure in the ribosome and contacts elongation factors in the vicinity of their GTP-binding site. In contrast, the GAC is mobile and we hypothesize that it interacts with the alpha helix D of the EF-Tu G-domain in the same way as with the alpha helix A of the G'-domain of EF-G. The mutual locations of these helices and GTP-binding sites in the structures of EF-Tu and EF-G are different. Thus, the orientation of the GAC relative to the SRL determines whether EF-G or EF-Tu will bind to the ribosome.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Binding Sites
  • Endoribonucleases / metabolism
  • Fungal Proteins / metabolism
  • GTP Phosphohydrolases / metabolism
  • Peptide Elongation Factor G / chemistry*
  • Peptide Elongation Factor G / metabolism*
  • Peptide Elongation Factor Tu / chemistry*
  • Peptide Elongation Factor Tu / metabolism*
  • Protein Conformation
  • Ribosomes / metabolism*

Substances

  • Fungal Proteins
  • Peptide Elongation Factor G
  • alpha-sarcin
  • Endoribonucleases
  • GTP Phosphohydrolases
  • Peptide Elongation Factor Tu