3D8X

Crystal Structure of Saccharomyces cerevisiae NDPPH Dependent Thioredoxin Reductase 1

Summary for 3D8X

• Entry DOI: 10.2210/pdb3d8x/pdb
• Descriptor: Thioredoxin reductase 1, FLAVIN-ADENINE DINUCLEOTIDE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: thioredoxin reductase, nadph, yeast, modpipe model of a6z, fad, flavoprotein, oxidoreductase, redox-active center
• Biological source: Saccharomyces cerevisiae
• Cellular location: Cytoplasm: P29509
• Total number of polymer chains: 2
• Total formula weight: 72642.39

Authors

Zhang, Z.Y.,Bao, R.,Yu, J.,Chen, Y.X.,Zhou, C.-Z. (deposition date: 2008-05-26, release date: 2008-12-09, Last modification date: 2024-10-16)

Primary citation

Zhang, Z.,Bao, R.,Zhang, Y.,Yu, J.,Zhou, C.-Z.,Chen, Y.
Crystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin
Biochim.Biophys.Acta, 1794:124-128, 2009

PubMed Abstract: Thioredoxin reductase (TrxR) is a member of the pyridine nucleotide-disulfide oxidoreductase family of the flavoenzymes. It can use a dithiol-disulfide active-site to transfer reducing equivalents from NADPH to thioredoxin (Trx), via the cofactor FAD. In Saccharomyces cerevisiae, the cytoplasmic thioredoxin reductase Trr1 plays an important role in multiple cellular events under the control of transcription factor Yap1 and/or Rho5. Here we present the crystal structure of Trr1 at the resolution of 2.8 A, the first fungal TrxR structure. Structural analysis shows it shares a very similar overall structure to Escherichia coli TrxR. However, fine comparisons indicate some distinct differences at the Trx recognition sites. These differences might be responsible to the species-specific recognition of Trx, which has been demonstrated by previous biochemical assays.

PubMed: 18930846
DOI: 10.1016/j.bbapap.2008.09.011

Experimental method

X-RAY DIFFRACTION (2.8 Å)