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.
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 |
|