1USP
Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans
Summary for 1USP
| Entry DOI | 10.2210/pdb1usp/pdb |
| Descriptor | ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, 2-cys peroxidase |
| Biological source | DEINOCOCCUS RADIODURANS More |
| Total number of polymer chains | 2 |
| Total formula weight | 29820.18 |
| Authors | Meunier-Jamin, C.,Kapp, U.,Leonard, G.,McSweeney, S. (deposition date: 2003-11-27, release date: 2004-04-08, Last modification date: 2024-10-16) |
| Primary citation | Meunier-Jamin, C.,Kapp, U.,Leonard, G.,Mcsweeney, S. The Structure of the Organic Hydroperoxide Resistance Protein from Deinococcus Radiodurans: Do Conformational Changes Facilitate Recycling of the Redox Disulfide? J.Biol.Chem., 279:25830-, 2004 Cited by PubMed 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. PubMed: 15054099DOI: 10.1074/JBC.M312983200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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