1qwi
From Proteopedia
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| - | [[Image:1qwi.jpg|left|200px]] | + | [[Image:1qwi.jpg|left|200px]] |
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| - | '''Crystal Structure of E. coli OsmC''' | + | {{Structure |
| + | |PDB= 1qwi |SIZE=350|CAPTION= <scene name='initialview01'>1qwi</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= OsmC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of E. coli OsmC''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QWI is a [ | + | 1QWI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14627744 14627744] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydroperoxide resistance]] | [[Category: hydroperoxide resistance]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:38 2008'' |
Revision as of 11:43, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Gene: | OsmC (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of E. coli OsmC
Overview
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.
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
Page seeded by OCA on Thu Mar 20 13:43:38 2008
