Structure of the Prx6‐subfamily 1‐Cys peroxiredoxin from Sulfolobus islandicus. Issue 6 (17th June 2019)

• Record Type: Journal Article
• Authors: Stroobants, Sander; Van Molle, Inge; Saidi, Queen; Jonckheere, Karl; Maes, Dominique; Peeters, Eveline
• Is Part Of: Acta crystallographica. Volume 75:Issue 6(2019:Jun.)
• Page Start: 428
• Page End: 434
• Publication Date: 2019-06-17
• Subjects: peroxiredoxins -- archaea -- Sulfolobus islandicus -- Prx6 -- chaperones; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X19006472
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of the 1‐Cys peroxiredoxin from S. islandicus is presented; it assembles into a ring‐shaped decamer composed of five homodimers. It is concluded that this Prx6‐like protein undergoes decamerization independently of arm‐domain cysteines. Abstract : Aerobic thermoacidophilic archaea belonging to the genus Sulfolobus harbor peroxiredoxins, thiol‐dependent peroxidases that assist in protecting the cells from oxidative damage. Here, the crystal structure of the 1‐Cys peroxiredoxin from Sulfolobus islandicus, named 1‐Cys SiPrx, is presented. A 2.75 Å resolution data set was collected from a crystal belonging to space group P 21 21 21, with unit‐cell parameters a = 86.8, b = 159.1, c = 189.3 Å, α = β = γ = 90°. The structure was solved by molecular replacement using the homologous Aeropyrum pernix peroxiredoxin (ApPrx) structure as a search model. In the crystal structure, 1‐Cys SiPrx assembles into a ring‐shaped decamer composed of five homodimers. This quaternary structure corresponds to the oligomeric state of the protein in solution, as observed by size‐exclusion chromatography. 1‐Cys SiPrx harbors only a single cysteine, which is the peroxidatic cysteine, and lacks both of the cysteines that are highly conserved in the C‐terminal arm domain in other archaeal Prx6‐subfamily proteins such as ApPrx and that are involved in the association of dimers into higher‐molecular‐weight decamers and dodecamers. It is thus concluded that the Sulfolobus Prx6‐subfamily protein undergoes decamerization independently of arm‐domain cysteines.