Literature summary for 1.15.1.2 extracted from

Bandeiras, T.M.; Romao, C.V.; Rodrigues, J.V.; Teixeira, M.; Matias, P.M.
Purification, crystallization and X-ray crystallographic analysis of Archaeoglobus fulgidus neelaredoxin (2010), Acta Crystallogr. Sect. F, 66, 316-319.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression in Escherichia coli strain BL21(DE3)-Gold	Archaeoglobus fulgidus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, mixing of 0.0001 ml of 15 mg/ml protein in 20 mM phosphate buffer, pH 7.5, and 150 mM NaCl, with 0.0001 ml of reservoir solution, equilibration against 0.1 ml reservoir solution, vapour diffusion method, 2-3 days, method variantions, overview. X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution, MAD method	Archaeoglobus fulgidus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
13700	-	x * 13700, recombinant enzyme	Archaeoglobus fulgidus

Organism

Organism	UniProt	Comment	Textmining
Archaeoglobus fulgidus	-	gene nlr	-

Subunits

Subunits	Comment	Organism
?	x * 13700, recombinant enzyme	Archaeoglobus fulgidus

Synonyms

Synonyms	Comment	Organism
neelaredoxin	-	Archaeoglobus fulgidus
Nlr	-	Archaeoglobus fulgidus
SOR	-	Archaeoglobus fulgidus

General Information

General Information	Comment	Organism
physiological function	superoxide reductases play a key role in defence mechanisms against toxic oxygen species. SOR is responsible for scavenging toxic superoxide anion radicals, catalysing the one-electron reduction of superoxide to hydrogen peroxide	Archaeoglobus fulgidus

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Release 2023.1 (January 2023)