Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface.

@article{Borgstahl1996HumanMM,
  title={Human mitochondrial manganese superoxide dismutase polymorphic variant Ile58Thr reduces activity by destabilizing the tetrameric interface.},
  author={Gloria E O Borgstahl and Hans E. Parge and Michael J. Hickey and Marvin J Johnson and M Boissinot and R. A. Hallewell and James R. Lepock and Diane E. Cabelli and John A. Tainer},
  journal={Biochemistry},
  year={1996},
  volume={35 14},
  pages={4287-97}
}
Human manganese superoxide dismutase (MnSOD) is a homotetrameric enzyme which protects mitochondria against oxygen-mediated free radical damage. Within each subunit, both the N-terminal helical hairpin and C-terminal alpha/beta domains contribute ligands to the catalytic manganese site. Two identical four-helix bundles, symmetrically assembled from the N-terminal helical hairpins, form a novel tetrameric interface that stabilizes the active sites. The 2.5 A crystallographic structure of the… CONTINUE READING