6q5v

Publication Abstract from PubMed

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 A resolution data set was collected from a crystal belonging to space group P212121, with unit-cell parameters a = 86.8, b = 159.1, c = 189.3 A, alpha = beta = gamma = 90 degrees . 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.

Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus.,Stroobants S, Van Molle I, Saidi Q, Jonckheere K, Maes D, Peeters E Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):428-434. doi:, 10.1107/S2053230X19006472. Epub 2019 May 13. PMID:31204689^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.