Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.
Models, Molecular
0301 basic medicine
0303 health sciences
Binding Sites
Erythrocytes
Protein Conformation
Superoxide Dismutase
Mercury
Iridium
3. Good health
Zinc
03 medical and health sciences
X-Ray Diffraction
Organometallic Compounds
Animals
Cattle
Histidine
Copper
Platinum
Protein Binding
DOI:
10.1073/pnas.72.4.1349
Publication Date:
2006-05-31T07:05:56Z
AUTHORS (4)
ABSTRACT
An electron density map at 3 angstrom resolution has been calculated for Cu2+, Zn2+ superoxide dismutase from bovine erythrocytes, and the course of the main chain has been traced. The dominant structural feature is an 8-stranded barrel of antiparallel beta-pleated sheet. There is one very short helical section and two long loops of non-repetitive structure. The Cu and Zn are bound between the loops and one side of the beta barrel and are about 6 Angstrom apart, with a common histidine ligand. The Cu has four histidine ligands in a somewhat distorted square plane, and the Zn has three histidines and an aspartate in approximately tetrahedral arrangement. The two coppers of a dimer are about 34 Angstrom apart. The two subunits have essentially the same conformation and have an extensive contact area that mainly involves hydrophobic side chain interactions. The overall folding pattern of the polypeptide chain is very similar to that of an immunoglobulin domain.
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