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Literature summary extracted from

  • Barbey, C.; Rouhier, N.; Haouz, A.; Navaza, A.; Jacquot, J.P.
    Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein from Thermotoga maritima (2008), Acta Crystallogr. Sect. F, 64, 29-31.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24 expressed in Escherichia coli BL21(DE3) cells Thermotoga maritima

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.24 sitting drop vapour diffusion method with 1.8 M ammonium sulfate, 0.1 M Tris-HCl pH 8.5, 7.5% (v/v) ethylene glycol Thermotoga maritima

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Thermotoga maritima
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.24 ammonium sulfate precipitation, ACA44 gel filtration, and DEAE Sephacel column chromatography Thermotoga maritima

Subunits

EC Number Subunits Comment Organism
1.11.1.24 hexamer trimer of homodimers , X-ray crystallography Thermotoga maritima

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 Prx belongs to the group of 1-Cys peroxiredoxins, Prx from Thermotoga maritima is part of a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus Thermotoga maritima

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.24 thioredoxin
-
 Thermotoga maritima