title: The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?
abstract: 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.
authors.affiliation: Macromolecular Crystallography Group, European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble Cedex, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Meunier-Jamin
authors.forename: Ulrike
authors.initials: U
authors.lastname: Kapp
authors.forename: Gordon A
authors.initials: GA
authors.lastname: Leonard
authors.forename: Seán
authors.initials: S
authors.lastname: McSweeney
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D034301:Deinococcus / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D029968:Escherichia coli Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D004220:Disulfides; D029968:Escherichia coli Proteins; C099394:osmC protein, E coli