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Open AccessArticle

C-Terminal Redox Domain of Arabidopsis APR1 Is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function

1
Department of Agricultural Chemistry, National Taiwan University, Taipei 10617, Taiwan, [email protected] (F.-F.C.)
2
Genome and Systems Biology Degree Program, National Taiwan University and Academia Sinica, Taipei 10617, Taiwan
*
Author to whom correspondence should be addressed.
These two authors contribute equally.
Antioxidants 2019, 8(10), 461; https://doi.org/10.3390/antiox8100461
Received: 1 September 2019 / Revised: 23 September 2019 / Accepted: 3 October 2019 / Published: 8 October 2019
(This article belongs to the Special Issue Thioredoxin Family Proteins)
Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5′-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated sulfate to sulfite, which requires glutathione. Previous studies have shown that the C-terminal domain of APR acts as a glutathione-dependent reductase. The crystal structure of the C-terminal redox domain of Arabidopsis APR1 (AtAPR1) shows a conserved α/β thioredoxin fold, but not a glutaredoxin fold. Further biochemical studies of the redox domain from AtAPR1 provided evidence to support the structural observation. Collectively, our results provide structural and biochemical information to explain how the thioredoxin fold exerts the glutaredoxin function in APR. View Full-Text
Keywords: APS reductase; redox domain; crystal structure; sulfur assimilation; redox potential APS reductase; redox domain; crystal structure; sulfur assimilation; redox potential
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Chen, F.-F.; Chien, C.-Y.; Cho, C.-C.; Chang, Y.-Y.; Hsu, C.-H. C-Terminal Redox Domain of Arabidopsis APR1 Is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function. Antioxidants 2019, 8, 461.

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