Crystallographic characterization and three-dimensional model of yeast Cu,Zn superoxide dismutase.
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.
Frigerio
F
F
Department of Genetics and Microbiology, University of Pavia, Italy.
Falconi
M
M
Gatti
G
G
Bolognesi
M
M
Desideri
A
A
Marmocchi
F
F
Rotilio
G
G
D000595:Amino Acid Sequence; D003196:Computer Graphics; D003461:Crystallography; D008958:Models, Molecular; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013329:Structure-Activity Relationship; D013482:Superoxide Dismutase
D013482:Superoxide Dismutase