1usp
From Proteopedia
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[[Category: 2-cys peroxidase]] | [[Category: 2-cys peroxidase]] | ||
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Revision as of 15:05, 5 November 2007
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ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN FROM DEINOCOCCUS RADIODURANS
Overview
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.
About this Structure
1USP is a Protein complex structure of sequences from Deinococcus radiodurans with GOL as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
The structure of the organic hydroperoxide resistance protein from Deinococcus radiodurans. Do conformational changes facilitate recycling of the redox disulfide?, Meunier-Jamin C, Kapp U, Leonard GA, McSweeney S, J Biol Chem. 2004 Jun 11;279(24):25830-7. Epub 2004 Mar 30. PMID:15054099
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