5YRY

Crystal structure of C-terminal redox domain of APR1 from Arabidopsis thaliana

5YRY の概要

• エントリーDOI: 10.2210/pdb5yry/pdb
• 分子名称: 5'-adenylylsulfate reductase 1, chloroplastic (2 entities in total)
• 機能のキーワード: redox domain, sulfer assimilatory, aps reductase, oxidoreductase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14132.12

構造登録者

Hsu, C.H. (登録日: 2017-11-11, 公開日: 2018-11-14, 最終更新日: 2024-03-27)

主引用文献

Chen, F.F.,Chien, C.Y.,Cho, C.C.,Chang, Y.Y.,Hsu, C.H.
C-terminal Redox Domain ofArabidopsisAPR1 is a Non-Canonical Thioredoxin Domain with Glutaredoxin Function.
Antioxidants (Basel), 8:-, 2019

PubMed Abstract: 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 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.

PubMed: 31597378
DOI: 10.3390/antiox8100461

実験手法

X-RAY DIFFRACTION (2.698 Å)