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M312983200v1
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Papers In Press, published online ahead of print March 30, 2004
J. Biol. Chem, 10.1074/jbc.M312983200
Submitted on November 30, 2003
Revised on March 29, 2004
Accepted on March 30, 2004

The structure of the organic hydroperoxide resistance protein from deinococcus radiodurans: Do conformational changes facilitate recycling of the redox disulphide?

Cecile Meunier-Jamin, Ulrike Kapp, Gordon A. Leonard, and Sean McSweeney

Macromolecular Crystallography, European Synchrotron Radiation Facility, Grenoble F-38043

Corresponding Author: seanmcs{at}esrf.fr

The three-dimensional structure of the Organic Hydroperoxide Resistance Protein (OHRP) from Deinococcus radiodurans as determined using single-crystal X-ray 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 disulphide moiety. It is postulated that the closed configuration is consistent with efficient catalysis of the reduction of organic hydroperoxides while 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 protei


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