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Literature summary for 1.15.1.1 extracted from

  • Roberts, B.R.; Tainer, J.A.; Getzoff, E.D.; Malencik, D.A.; Anderson, S.R.; Bomben, V.C.; Meyers, K.R.; Karplus, P.A.; Beckman, J.S.
    Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS (2007), J. Mol. Biol., 373, 877-890.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
purified zinc-deficient mutant enzyme, 0.002 ml of solution containing 15.7 mg/ml protein in 50 mM Na/K phosphate, pH 7.7, is mixed with 0.002 ml of reservoir solution containing 2.45 M ammonium sulfate, 200 mM NaCl in 50 mM Tris, pH 7.5, room temperature, less than 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modelling Homo sapiens

Protein Variants

Protein Variants Comment Organism
C111S site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit Homo sapiens
D124N site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit Homo sapiens
D124N/C111S site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit Homo sapiens
D83S site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit Homo sapiens
D83S/C111S site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit Homo sapiens
H80S/D83S site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit Homo sapiens
H80S/D83S/C6A/C111S site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit Homo sapiens
additional information construction of a zinc-deficient enzyme, structure analysis, the loss of zinc from SOD is potentially important for both the aggregation and zinc-deficient Cu,Zn-SOD hypotheses, and leads to an altered dimer, phenotypes, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ a Cu,ZnSOD with 1.07 Cu2+ per enzyme subunit, binding structure, position of Cu2+ in the Zn2+-deficient enzyme A chain active site, overview, physiologic function in Cu,Zn-SOD, overview Homo sapiens
Zn2+ a Cu,ZnSOD with 1.18 Zn2+ per enzyme subunit, binding structure, overview Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
O2.- + H+ Homo sapiens
-
O2 + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P00441
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O2.- + H+
-
Homo sapiens O2 + H2O2
-
?

Subunits

Subunits Comment Organism
More asymmetric structure of the zinc-deficient enzyme, overview Homo sapiens

Synonyms

Synonyms Comment Organism
copper, zinc superoxide dismutase
-
Homo sapiens