Literature summary for 1.11.1.24 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.

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Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Thermotoga maritima	-	-	-

Purification (Commentary)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
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

Cofactor	Comment	Organism	Structure
thioredoxin	-	Thermotoga maritima

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Release 2023.1 (January 2023)