Crystal structure analysis of the translation factor RF3 (release factor 3)

FEBS Lett. 2012 Oct 19;586(20):3705-9. doi: 10.1016/j.febslet.2012.08.029. Epub 2012 Sep 6.

Abstract

The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3',5'-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0Å, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.

MeSH terms

  • Crystallography, X-Ray
  • Desulfovibrio vulgaris
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Guanosine Diphosphate / metabolism
  • Guanosine Triphosphate / metabolism
  • Models, Molecular
  • Peptide Termination Factors / chemistry*
  • Peptide Termination Factors / metabolism*
  • Protein Conformation

Substances

  • Escherichia coli Proteins
  • Peptide Termination Factors
  • prfA protein, E coli
  • prfC protein, E coli
  • Guanosine Diphosphate
  • Guanosine Triphosphate

Associated data

  • PDB/3VQT
  • PDB/3VR1