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
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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