The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?

J Biol Chem. 2004 Jun 11;279(24):25830-7. doi: 10.1074/jbc.M312983200. Epub 2004 Mar 30.


The three-dimensional structure of the organic hydroperoxide resistance protein (OHRP) from Deinococcus radiodurans as determined using single crystal xray diffraction techniques is reported. Comparison of the structure with that obtained for OHRP from Pseudomonas aeruginosa reveals that the polypeptide chain of OHRPs can adopt two significantly different conformations ("in" and "out") in the region of the active site disulfide moiety. It is postulated that the closed configuration is consistent with efficient catalysis of the reduction of organic hydroperoxides, whereas the open form is required for enzyme recycling. Comparison of the structures of OHRP and that of the osmotically induced protein C (OsmC) from Mycoplasma pneumoniae shows that OHRPs and OsmCs are structurally homologous, perhaps indicating related functions for the two families of proteins.

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Crystallization
  • Deinococcus / chemistry*
  • Disulfides / chemistry
  • Escherichia coli Proteins / chemistry
  • Molecular Sequence Data
  • Protein Conformation


  • Bacterial Proteins
  • Disulfides
  • Escherichia coli Proteins
  • osmC protein, E coli

Associated data

  • PDB/1USP