6ky4
Crystal structure of Sulfiredoxin from Arabidopsis thaliana
Structural highlights
FunctionSRX_ARATH Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in a peroxiredoxin. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase. Required to switch on the antioxidant pathway to regenerate the oxidative damage. In mitochondrion, catalyzes the retroreduction of the inactive sulfinic form of atypical Prx IIF using thioredoxin as reducing agent.[1] [2] Publication Abstract from PubMedTypical 2-cysteine peroxiredoxins (2-Cys Prxs) are critical peroxidase sensors and could be deactivated by the hyperoxidation under oxidative stress. In plants, 2-Cys Prxs present at a high level in chloroplasts and are repaired by Sulfiredoxin. Whereas many studies have explored the mechanism of Sulfiredoxin from Homo sapiens (HsSrx), the molecular mechanism of Sulfiredoxin in plants with unique photosynthesis remains unclear. Here we report the crystal structure of Sulfiredoxin from Arabidopsis thaliana (AtSrx), which displayed a typical ParB/Srx fold with an ATP bound at a conservative nucleotide binding motif GCHR. Both the ADP binding pocket and the putative AtSrx-AtPrxA interaction surface of AtSrx are more positively charged comparing to HsSrx, suggesting a robust mechanism of AtSrx. These features illustrate the unique mechanisms of AtSrx, which are vital for figure out the strategies of plants to cope with oxidation stress. The crystal structure of sulfiredoxin from Arabidopsis thaliana revealed a more robust antioxidant mechanism in plants.,Liu M, Wang J, Li X, Sylvanno MJ, Li M, Zhang M, Wang M Biochem Biophys Res Commun. 2019 Oct 8. pii: S0006-291X(19)31923-0. doi:, 10.1016/j.bbrc.2019.10.034. PMID:31604522[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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