2A4H

Solution structure of Sep15 from Drosophila melanogaster

2A4H の概要

• エントリーDOI: 10.2210/pdb2a4h/pdb
• 関連するPDBエントリー: 2A2P
• NMR情報: BMRB: 6738
• 分子名称: Selenoprotein Sep15 (1 entity in total)
• 機能のキーワード: selenoprotein, redox, oxidoreductase
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14319.98

構造登録者

Ferguson, A.D.,Labunskyy, V.M.,Fomenko, D.E.,Chelliah, Y.,Amezcua, C.A.,Rizo, J.,Gladyshev, V.N.,Deisenhofer, J. (登録日: 2005-06-28, 公開日: 2005-12-13, 最終更新日: 2024-11-20)

主引用文献

Ferguson, A.D.,Labunskyy, V.M.,Fomenko, D.E.,Chelliah, Y.,Amezcua, C.A.,Rizo, J.,Gladyshev, V.N.,Deisenhofer, J.
NMR Structures of the Selenoproteins Sep15 and SelM Reveal Redox Activity of a New Thioredoxin-like Family.
J.Biol.Chem., 281:3536-3543, 2006

PubMed Abstract: Selenium has significant health benefits, including potent cancer prevention activity and roles in immune function and the male reproductive system. Selenium-containing proteins, which incorporate this essential micronutrient as selenocysteine, are proposed to mediate the positive effects of dietary selenium. Presented here are the solution NMR structures of the selenoprotein SelM and an ortholog of the selenoprotein Sep15. These data reveal that Sep15 and SelM are structural homologs that establish a new thioredoxin-like protein family. The location of the active-site redox motifs within the fold together with the observed localized conformational changes after thiol-disulfide exchange and measured redox potential indicate that they have redox activity. In mammals, Sep15 expression is regulated by dietary selenium, and either decreased or increased expression of this selenoprotein alters redox homeostasis. A physiological role for Sep15 and SelM as thiol-disulfide oxidoreductases and their contribution to the quality control pathways of the endoplasmic reticulum are discussed.

PubMed: 16319061
DOI: 10.1074/jbc.M511386200

実験手法

SOLUTION NMR