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J. Biol. Chem., Vol. 279, Issue 24, 25830-25837, June 11, 2004

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The Structure of the Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans

DO CONFORMATIONAL CHANGES FACILITATE RECYCLING OF THE REDOX DISULFIDE?^*

Cécile Meunier-Jamin, Ulrike Kapp, Gordon A. Leonard, and Seán McSweeney

From the Macromolecular Crystallography Group, European Synchrotron Radiation Facility, B.P. 220, F-38043 Grenoble Cedex, France

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.

Received for publication, November 30, 2003 , and in revised form, March 29, 2004.

The atomic coordinates and structure factors (code 1USP) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 33-4-76-88-23-62; Fax: 33-4-76-88-21-60; E-mail: seanmcs{at}esrf.fr.

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