Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.

• DOI: 10.1073/pnas.72.4.1349
• Publication Date: 2006-05-31T07:05:56Z
• Authors: J Richardson; K A Thomas; B H Rubin; D C Richardson
• Keywords: Antiparallel (mathematics); Multiple isomorphous replacement; Beta sheet

An electron density map at 3 angstrom resolution has been calculated for Cu2+, Zn2+ superoxide dismutase from bovine erythrocytes, and the course of main chain traced. The dominant structural feature is an 8-stranded barrel antiparallel beta-pleated sheet. There one very short helical section two long loops non-repetitive structure. Cu Zn are bound between side beta about 6 Angstrom apart, with a common histidine ligand. four ligands in somewhat distorted square plane, three histidines aspartate approximately tetrahedral arrangement. coppers dimer 34 apart. subunits have essentially same conformation extensive contact area that mainly involves hydrophobic interactions. overall folding pattern polypeptide similar to immunoglobulin domain.