Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC Journal Article
| Authors: | Lesniak, J.; Barton, W. A.; Nikolov, D. B. |
| Article Title: | Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC |
| Abstract: | The osmotically inducible protein OsmC, like its better-characterized homolog, the organic hydroperoxide protein Ohr, is involved in defense against oxidative stress caused by exposure to organic hydroperoxides. The crystal structure of Escherichia coli OsmC reported here reveals that the protein is a tightly folded domain-swapped dimer with two active sites located at the monomer interface on opposite sides of the molecule. We demonstrate that OsmC preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide. On the basis of structural and enzymatic similarities, we propose that the OsmC catalytic mechanism is analogous to that of the Ohr proteins and of the structurally unrelated peroxiredoxins, directly using highly reactive cysteine thiol groups to elicit hydroperoxide reduction. |
| Keywords: | controlled study; unclassified drug; nonhuman; protein conformation; peroxidase; protein; bacteria (microorganisms); bacterial protein; amino acid sequence; molecular sequence data; sequence homology, amino acid; nucleotide sequence; escherichia coli; models, molecular; crystallography, x-ray; hydrogen peroxide; oxidative stress; catalysis; sequence homology; peroxiredoxin; enzyme structure; catalyst; cysteine; escherichia coli proteins; reduction; peroxiredoxins; negibacteria; priority journal; article; organic hydroperoxides; hydroperoxide; protein ohr; protein osmc; thiol group; osmosis |
| Journal Title: | Protein Science |
| Volume: | 12 |
| Issue: | 12 |
| ISSN: | 0961-8368 |
| Publisher: | Wiley Blackwell |
| Date Published: | 2003-12-01 |
| Start Page: | 2838 |
| End Page: | 2843 |
| Language: | English |
| DOI: | 10.1110/ps.03375603 |
| PUBMED: | 14627744 |
| PROVIDER: | scopus |
| PMCID: | PMC2366992 |
| DOI/URL: | |
| Notes: | Export Date: 12 September 2014 -- Molecular Sequence Numbers: GENBANK: AAG54420, AAG54962, AAG55051; -- Source: Scopus |
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