Ontology highlight
ABSTRACT:
SUBMITTER: Parge HE
PROVIDER: S-EPMC49447 | biostudies-other | 1992 Jul
REPOSITORIES: biostudies-other
Proceedings of the National Academy of Sciences of the United States of America 19920701 13
Superoxide dismutase enzymes protect aerobic organisms from oxygen-mediated free-radical damage. Crystallographic structures of recombinant human Cu,Zn superoxide dismutase have been determined, refined, and analyzed at 2.5 A resolution for wild-type and a designed thermostable double-mutant enzyme (Cys-6----Ala, Cys-111----Ser). The 10 subunits (five dimers) in the crystallographic asymmetric unit form an unusual stable open lattice with 80-A-diameter channels. The 10 independently fit and refi ...[more]