1QWI

Crystal Structure of E. coli OsmC

1QWI の概要

• エントリーDOI: 10.2210/pdb1qwi/pdb
• 関連するPDBエントリー: 1N2F
• 分子名称: osmotically inducible protein (2 entities in total)
• 機能のキーワード: hydroperoxide resistance, hydroperoxide reductase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P0C0L2
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61103.27

構造登録者

Lesniak, J.,Barton, W.A.,Nikolov, D.B. (登録日: 2003-09-02, 公開日: 2003-12-16, 最終更新日: 2011-07-13)

主引用文献

Lesniak, J.,Barton, W.A.,Nikolov, D.B.
Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC
Protein Sci., 12:2838-2843, 2003

PubMed 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.

PubMed: 14627744
DOI: 10.1110/ps.03375603

実験手法

X-RAY DIFFRACTION (1.8 Å)