2A4H
Solution structure of Sep15 from Drosophila melanogaster
Summary for 2A4H
| Entry DOI | 10.2210/pdb2a4h/pdb |
| Related | 2A2P |
| NMR Information | BMRB: 6738 |
| Descriptor | Selenoprotein Sep15 (1 entity in total) |
| Functional Keywords | selenoprotein, redox, oxidoreductase |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 14319.98 |
| Authors | Ferguson, A.D.,Labunskyy, V.M.,Fomenko, D.E.,Chelliah, Y.,Amezcua, C.A.,Rizo, J.,Gladyshev, V.N.,Deisenhofer, J. (deposition date: 2005-06-28, release date: 2005-12-13, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 16319061DOI: 10.1074/jbc.M511386200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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