C-Terminal Redox Domain of <i>Arabidopsis</i> APR1 Is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function
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 glutathi...
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| Main Authors: | , , , , |
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| Format: | Book |
| Published: |
MDPI AG,
2019-10-01T00:00:00Z.
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| Online Access: | Connect to this object online. |
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| Summary: | 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 <i>Arabidopsis</i> 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. |
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| Item Description: | 2076-3921 10.3390/antiox8100461 |