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6Q5V

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

Replaces:  6GWWReplaces:  6FEU
Summary for 6Q5V
Entry DOI10.2210/pdb6q5v/pdb
DescriptorPeroxiredoxin (1 entity in total)
Functional Keywordsarchaea, peroxiredoxin, sulfolobus islandicus, oxidoreductase
Biological sourceSulfolobus islandicus (strain REY15A)
Total number of polymer chains10
Total formula weight246766.54
Authors
Stroobants, S.,Maes, D.,Peeters, E.,van Molle, I. (deposition date: 2018-12-09, release date: 2019-05-29, Last modification date: 2024-01-24)
Primary citationStroobants, S.,Van Molle, I.,Saidi, Q.,Jonckheere, K.,Maes, D.,Peeters, E.
Structure of the Prx6-subfamily 1-Cys peroxiredoxin from Sulfolobus islandicus.
Acta Crystallogr.,Sect.F, 75:428-434, 2019
Cited by
PubMed 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 P222, 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.
PubMed: 31204689
DOI: 10.1107/S2053230X19006472
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.747 Å)
Structure validation

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