5B8A

Crystal structure of oxidized chimeric EcAhpC1-186-YFSKHN

5B8A の概要

• エントリーDOI: 10.2210/pdb5b8a/pdb
• 関連するPDBエントリー: 5B8B
• 分子名称: Alkyl hydroperoxide reductase subunit C,Peroxiredoxin-2, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: alkylhydroperoxide reductase, ahpc, peroxiredoxins, chimeric, oxidoreductase
• 由来する生物種: Escherichia coli (strain K12); 詳細
• 細胞内の位置: Cytoplasm: P32119
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 218756.61

構造登録者

Kamariah, N.,Sek, M.F.,Eisenhaber, B.,Eisenhaber, F.,Gruber, G. (登録日: 2016-06-14, 公開日: 2017-02-01, 最終更新日: 2023-11-08)

主引用文献

Kamariah, N.,Sek, M.F.,Eisenhaber, B.,Eisenhaber, F.,Gruber, G.
Transition steps in peroxide reduction and a molecular switch for peroxide robustness of prokaryotic peroxiredoxins.
Sci Rep, 6:37610-37610, 2016

PubMed Abstract: In addition to their antioxidant function, the eukaryotic peroxiredoxins (Prxs) facilitate peroxide-mediated signaling by undergoing controlled inactivation by peroxide-driven over-oxidation. In general, the bacterial enzyme lacks this controlled inactivation mechanism, making it more resistant to high HO concentrations. During peroxide reduction, the active site alternates between reduced, fully folded (FF), and oxidized, locally unfolded (LU) conformations. Here we present novel insights into the divergence of bacterial and human Prxs in robustness and sensitivity to inactivation, respectively. Structural details provide new insights into sub-steps during the catalysis of peroxide reduction, enabling the transition from an FF to a LU conformation. Complementary to mutational and enzymatic results, these data unravel the essential role of the C-terminal tail of bacterial Prxs to act as a molecular switch, mediating the transition from an FF to a LU state. In addition, we propose that the C-terminal tail has influence on the propensity of the disulphide bond formation, indicating that as a consequence on the robustness and sensitivity to over-oxidation. Finally, a physical linkage between the catalytic site, the C-terminal tail and the oligomer interface is described.

PubMed: 27892488
DOI: 10.1038/srep37610

実験手法

X-RAY DIFFRACTION (2.7 Å)