Crystal Structure of Drosophila Thioredoxin Reductase, wild-typeCrystal Structure of Drosophila Thioredoxin Reductase, wild-type
Structural highlights
3dh9 is a 2 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[TRXR1_DROME] Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms.[1][2][3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Kanzok SM, Fechner A, Bauer H, Ulschmid JK, Muller HM, Botella-Munoz J, Schneuwly S, Schirmer R, Becker K. Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster. Science. 2001 Jan 26;291(5504):643-6. PMID:11158675 doi:http://dx.doi.org/10.1126/science.291.5504.643
↑Missirlis F, Phillips JP, Jackle H. Cooperative action of antioxidant defense systems in Drosophila. Curr Biol. 2001 Aug 21;11(16):1272-7. PMID:11525742
↑Missirlis F, Ulschmid JK, Hirosawa-Takamori M, Gronke S, Schafer U, Becker K, Phillips JP, Jackle H. Mitochondrial and cytoplasmic thioredoxin reductase variants encoded by a single Drosophila gene are both essential for viability. J Biol Chem. 2002 Mar 29;277(13):11521-6. Epub 2002 Jan 16. PMID:11796729 doi:http://dx.doi.org/10.1074/jbc.M111692200
