Literature summary for 1.15.1.2 extracted from

Pinho, F.G.; Romao, C.V.; Pinto, A.F.; Saraiva, L.M.; Huber, H.; Matias, P.M.; Teixeira, M.; Bandeiras, T.M.
Cloning, purification, crystallization and X-ray crystallographic analysis of Ignicoccus hospitalis neelaredoxin (2010), Acta Crystallogr. Sect. F, 66, 605-607.

Cloned(Commentary)

Cloned (Comment)	Organism
gene nlr, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli strain XL-2 Blue, expression in Escherichia coli strain BL21(DE3)	Ignicoccus hospitalis

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of purified recombinant oxidized 1Fe-SOR at room temperature, by sitting-drop vapour-diffusion method, mixing of 15 mg/ml protein in 20 mM Tris-HCl pH 7.2, 150 mM NaCl, with different drop mixing ratios of protein and reservoir solutions, method optimization to hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution with 0.0005 ml of reservoir solution containing 85 mM Tris, pH 8.5, 8.5 mM NiCl2, 15% v/v PEG 2000 MME, and 15% v/v glycerol, X-ray diffraction structure determination and analysis of the blue crystals at 2.4 A resolution	Ignicoccus hospitalis

Crystallization (Comment)

Organism

crystallization of purified recombinant oxidized 1Fe-SOR at room temperature, by sitting-drop vapour-diffusion method, mixing of 15 mg/ml protein in 20 mM Tris-HCl pH 7.2, 150 mM NaCl, with different drop mixing ratios of protein and reservoir solutions, method optimization to hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution with 0.0005 ml of reservoir solution containing 85 mM Tris, pH 8.5, 8.5 mM NiCl2, 15% v/v PEG 2000 MME, and 15% v/v glycerol, X-ray diffraction structure determination and analysis of the blue crystals at 2.4 A resolution

Ignicoccus hospitalis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe	the enzyme contains a catalytic nonheme iron centre coordinated by four histidine ligands and one cysteine ligand	Ignicoccus hospitalis
additional information	SORs can be classified as 1Fe-SORs, or neelaredoxins, or as 2Fe-SORs, or desulfoferrodoxins, according to the number of metal centres	Ignicoccus hospitalis

Organism

Organism	UniProt	Comment	Textmining
Ignicoccus hospitalis	-	gene nlr	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli by anion exchange chromatography, ultrafiltration, and gel filtration	Ignicoccus hospitalis

Synonyms

Synonyms	Comment	Organism
1Fe-SOR	-	Ignicoccus hospitalis
More	superoxide reductases, SORs, constitute a family of enzymes that are able to scavenge superoxide anion through its reduction only, distinct from superoxide dismutases	Ignicoccus hospitalis
neelaredoxin-type SOR	-	Ignicoccus hospitalis
Nlr	-	Ignicoccus hospitalis

General Information

General Information	Comment	Organism
additional information	SORs can be classified as 1Fe-SORs, or neelaredoxins, or as 2Fe-SORs, or desulfoferrodoxins, according to the number of metal centres. Both share a common active site in which the reduction of superoxide anion occurs. This site is composed of a pentacoordinated iron with four equatorial histidine imidazoles and one axial cysteine sulfur in a square-pyramidal geometry [Fe(Cys)(His)4]	Ignicoccus hospitalis
physiological function	the neelaredoxin-type SOR keeps toxic oxygen species levels under control. SORs are involved in scavenging superoxide radicals from the cell by catalyzing the reduction of superoxide to hydrogen peroxide	Ignicoccus hospitalis