1qwi
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1qwi |SIZE=350|CAPTION= <scene name='initialview01'>1qwi</scene>, resolution 1.8Å | |PDB= 1qwi |SIZE=350|CAPTION= <scene name='initialview01'>1qwi</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= OsmC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= OsmC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1n2f|1N2F]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwi OCA], [http://www.ebi.ac.uk/pdbsum/1qwi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qwi RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: hydroperoxide resistance]] | [[Category: hydroperoxide resistance]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:57 2008'' |
Revision as of 20:19, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | OsmC (Escherichia coli) | ||||||
| Related: | 1N2F
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 23:19:57 2008
