1qwi

<table><tr><td colspan='2'>[[1qwi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QWI FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n2f|1n2f]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OsmC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwi OCA], [http://pdbe.org/1qwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qwi RCSB], [http://www.ebi.ac.uk/pdbsum/1qwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwi ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/OSMC_ECOLI OSMC_ECOLI]] Preferentially metabolizes organic hydroperoxides over inorganic hydrogen peroxide.<ref>PMID:14627744</ref>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:14627744</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1qwi" style="background-color:#fffaf0;"></div>

[[Category: Bacillus coli migula 1895]]

[[Category: Barton, W A]]

[[Category: Lesniak, J]]

[[Category: Nikolov, D B]]

[[Category: Hydroperoxide resistance]]