1qwi

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{{STRUCTURE_1qwi| PDB=1qwi | SCENE= }}
{{STRUCTURE_1qwi| PDB=1qwi | SCENE= }}
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'''Crystal Structure of E. coli OsmC'''
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===Crystal Structure of E. coli OsmC===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_14627744}}
==About this Structure==
==About this Structure==
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[[Category: Nikolov, D B.]]
[[Category: Nikolov, D B.]]
[[Category: Hydroperoxide resistance]]
[[Category: Hydroperoxide resistance]]
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Revision as of 22:58, 27 July 2008

Image:1qwi.png

Template:STRUCTURE 1qwi

Crystal Structure of E. coli OsmC

Template:ABSTRACT PUBMED 14627744

About this Structure

1QWI is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC., Lesniak J, Barton WA, Nikolov DB, Protein Sci. 2003 Dec;12(12):2838-43. PMID:14627744

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