Reference: Frigerio F, et al. (1989) Crystallographic characterization and three-dimensional model of yeast Cu,Zn superoxide dismutase. Biochem Biophys Res Commun 160(2):677-81

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Abstract


The Cu,Zn superoxide dismutase from yeast was crystallized in the orthorhombic space group P21212 with unit cell dimension a = 105.1 A,b = 142.2 A, c = 62.1 A. The crystals grow in 25 mM citrate, 10 mM phosphate buffer pH 6.5, and 6% (W/V) polyethylene glycol, with a Vm of 3,4 A3/dalton, for two dimers/asymmetric unit. The crystals were unstable in the mother liquor, but were stabilized by transfer to a 35% polyethylene glycol solution. This crystalline form diffracts at high resolution and is suitable for determination of the atomic structure. The three dimensional structure of the yeast enzyme could be model-built by computer graphics techniques using the bovine enzyme atomic coordinates as template. The proposed model requires removal of some salt bridges and non equivalence of the metal-binding sites in the subunits, in line with reported functional properties of the yeast enzyme.

Reference Type
Journal Article
Authors
Frigerio F, Falconi M, Gatti G, Bolognesi M, Desideri A, Marmocchi F, Rotilio G
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