6q5v | pdb_00006q5v

1-Cys SiPrx, a Prx6-family 1-Cys peroxiredoxin of the thermoacidophilic archaeon Sulfolobus islandicus

spinqualitylabelsall models 6q5v, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q5v is a 10 chain structure with sequence from Sulir. This structure supersedes the now removed PDB entries 6gww and 6feu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: SiRe_0346 (SULIR) Activity: Peroxiredoxin, with EC number 1.11.1.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [F0NEA3_SULIR] 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.[HAMAP-Rule:MF_00401] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peroxiredoxin

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