ArticleActa crystallographica. Section D, Biological crystallography2009
Structure of Hordeum vulgare NADPH-dependent thioredoxin reductase 2. Unwinding the reaction mechanism.
Article in Acta crystallographica. Section D, Biological crystallography, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- New Insights into the Potential of Endogenous Redox Systems in Wheat Bread Dough.Antioxidants (Basel, Switzerland) · 2018Article
- The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage.Scientific reports · 2017Article
- X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action.Journal of structural biology · 2016Article
- The structural basis of an NADP⁺-independent dithiol oxidase in FK228 biosynthesis.Scientific reports · 2014Article
- IruO is a reductase for heme degradation by IsdI and IsdG proteins in Staphylococcus aureus.The Journal of biological chemistry · 2013Article
- The barley grain thioredoxin system - an update.Frontiers in plant science · 2013Article
- Crystallization and diffraction analysis of thioredoxin reductase from Streptomyces coelicolor.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thioredoxins (Trxs) are protein disulfide reductases that regulate the intracellular redox environment and are important for seed germination in plants. Trxs are in turn regulated by NADPH-dependent thioredoxin reductases (NTRs), which provide reducing equivalents to Trx using NADPH to recycle Trxs to the active form. Here, the first crystal structure of a cereal NTR, HvNTR2 from Hordeum vulgare (barley), is presented, which is also the first structure of a monocot plant NTR. The structure was determined at 2.6 A resolution and refined to an R(cryst) of 19.0% and an R(free) of 23.8%. The dimeric protein is structurally similar to the structures of AtNTR-B from Arabidopsis thaliana and other known low-molecular-weight NTRs. However, the relative position of the two NTR cofactor-binding domains, the FAD and the NADPH domains, is not the same. The NADPH domain is rotated by 25 degrees and bent by a 38% closure relative to the FAD domain in comparison with AtNTR-B. The structure may represent an intermediate between the two conformations described previously: the flavin-oxidizing (FO) and the flavin-reducing (FR) conformations. Here, analysis of interdomain contacts as well as phylogenetic studies lead to the proposal of a new reaction scheme in which NTR-Trx interactions mediate the FO to FR transformation.
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