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Literature summary extracted from

  • Esposito, L.; Seydel, A.; Aiello, R.; Sorrentino, G.; Cendron, L.; Zanotti, G.; Zagari, A.
    The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension (2008), Biochim. Biophys. Acta, 1784, 1601-1606.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.15.1.1 gene sodB, overexpression of the His6-tagged type A isozyme in Escherichia coli strain BL21(DE3) Helicobacter pylori

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.15.1.1 recombinant His6-tagged enzyme, hanging drop vapor diffusion method, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, at 23°C, mixing of 0.001 ml protein solution with 0.001 ml precipitant solution containing 1.9 M ammonium sulfate in 0.2 M Tris-HCl buffer, pH 8.0, X-ray diffraction structure determination and analysis at 2.4 A resolution, modelling Helicobacter pylori

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.15.1.1 Fe2+ Fe-SOD contains 1 Fe2+ per subunit Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.15.1.1 O2.- + H+ Helicobacter pylori a key enzyme for fighting oxidative stress O2 + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.15.1.1 Helicobacter pylori
-
 contains a single type A isozyme Fe-SOD encoded by gene sodB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.15.1.1 recombinant His6-tagged type A isozyme from Escherichia coli strain BL21(DE3) by His-trap affinity chromatography and gel filtration Helicobacter pylori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.15.1.1 O2.- + H+
-
 Helicobacter pylori O2 + H2O2
-
 ?
1.15.1.1 O2.- + H+ a key enzyme for fighting oxidative stress Helicobacter pylori O2 + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.15.1.1 dimer the homodimer contains an extended C-terminal tail comprising residues 193-213. Dimer interface and domain interface structure analysis: the shortest domain contacts involve residues Phe17, Leu52, Phe53, Tyr71, and Phe75 on one domain and Val145, Pro151, Val154, Tyr173, Phe177, His180, Cys189, Leu198, Ile205, and His210 on the other domain, and the dimer interface is stabilized by 10 hydrogen bonds and approximately 102 non-bonded contacts, involving 32 residues from both chains, overview Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
1.15.1.1 SOD
-
 Helicobacter pylori