Structural highlights
Function
[BAS1A_ARATH] Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. May be an antioxidant enzyme particularly in the developing shoot and photosynthesizing leaf.[1]
Publication Abstract from PubMed
Peroxiredoxins (Prxs), a large family of antioxidant enzymes, are abundant in all living organisms. Peroxiredoxin A (PrxA) from Arabidopsis thaliana belongs to the typical 2-Cys Prx family and is localized in the chloroplast. This article reports the crystal structure of a PrxA C119S mutant refined to 2.6 A resolution. The protein exists as a decamer both in the crystal structure and in solution. The structure is in the reduced state suitable for the approach of peroxide, though conformational changes are needed for the resolving process.
Crystal structure of Arabidopsis thaliana peroxiredoxin A C119S mutant.,Yang Y, Cai W, Wang J, Pan W, Liu L, Wang M, Zhang M Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):625-631. doi:, 10.1107/S2053230X18010920. Epub 2018 Sep 19. PMID:30279313[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Broin M, Cuine S, Eymery F, Rey P. The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin involved in the protection of the photosynthetic apparatus against oxidative damage. Plant Cell. 2002 Jun;14(6):1417-32. PMID:12084836
- ↑ Yang Y, Cai W, Wang J, Pan W, Liu L, Wang M, Zhang M. Crystal structure of Arabidopsis thaliana peroxiredoxin A C119S mutant. Acta Crystallogr F Struct Biol Commun. 2018 Oct 1;74(Pt 10):625-631. doi:, 10.1107/S2053230X18010920. Epub 2018 Sep 19. PMID:30279313 doi:http://dx.doi.org/10.1107/S2053230X18010920
