Molecular recognition between Escherichia coli enolase and ribonuclease E

Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):1036-40. doi: 10.1107/S0907444910030015. Epub 2010 Aug 13.

Abstract

In Escherichia coli and many other bacterial species, the glycolytic enzyme enolase is a component of the multi-enzyme RNA degradosome, an assembly that is involved in RNA processing and degradation. Enolase is recruited into the degradosome through interactions with a small recognition motif located within the degradosome-scaffolding domain of RNase E. Here, the crystal structure of enolase bound to its cognate site from RNase E (residues 823-850) at 1.9 A resolution is presented. The structure suggests that enolase may help to organize an adjacent conserved RNA-binding motif in RNase E.

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Endoribonucleases / chemistry*
  • Endoribonucleases / metabolism
  • Escherichia coli / enzymology*
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphopyruvate Hydratase / chemistry*
  • Phosphopyruvate Hydratase / metabolism
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • Protein Structure, Quaternary
  • Sequence Alignment

Substances

  • Endoribonucleases
  • ribonuclease E
  • Phosphopyruvate Hydratase