Download MendeleyCrystal structure of Saccharomyces cerevisiae cytoplasmic thioredoxin reductase Trr1 reveals the structural basis for species-specific recognition of thioredoxin
Zhang, Z., Bao, R., Zhang, Y., Yu, J., Zhou, C.-Z., Chen, Y.(2009) Biochim Biophys Acta 1794: 124-128
- PubMed: 18930846
- DOI: https://doi.org/10.1016/j.bbapap.2008.09.011
- Primary Citation of Related Structures:
3D8X - 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.
Organizational Affiliation:
Protein Research Institute, Tongji University, Shanghai 200092, People's Republic of China.
