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Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin

Mol Cell. 2005 Aug 19;19(4):497-509. doi: 10.1016/j.molcel.2005.07.004.

Abstract

The eubacterial chromosome encodes various addiction modules that control global levels of translation through RNA degradation. Crystal structures of the Escherichia coli YefM2 (antitoxin)-YoeB (toxin) complex and the free YoeB toxin have been determined. The structure of the heterotrimeric complex reveals an asymmetric disorder-to-order recognition strategy, in which one C terminus of the YefM homodimer exclusively interacts with an atypical microbial ribonuclease (RNase) fold of YoeB. Comparison with the YefM-free YoeB structure indicates a conformational rearrangement of the RNase catalytic site of YoeB, induced by interaction with YefM. Complementary biochemical experiments demonstrate that the YoeB toxin has an in vitro RNase activity that preferentially cleaves at the 3' end of purine ribonucleotides.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / genetics
  • Bacterial Toxins / metabolism*
  • Catalytic Domain / physiology*
  • Crystallography, X-Ray
  • Dimerization
  • Enzyme Activation
  • Escherichia coli K12 / genetics
  • Escherichia coli K12 / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Ribonucleases / chemistry*
  • Ribonucleases / genetics
  • Sequence Alignment
  • Surface Properties

Substances

  • Bacterial Toxins
  • Escherichia coli Proteins
  • YefM protein, E coli
  • YoeB protein, E coli
  • Ribonucleases

Associated data

  • PDB/2A6Q
  • PDB/2A6R
  • PDB/2A6S