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1: Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13.Click here to read Links
Erratum in:
Proc Natl Acad Sci U S A 1992 Nov 15;89(22):11106.

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.

Parge HE, Hallewell RA, Tainer JA.

Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.

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 refined subunits provide high accuracy, error analysis, and insights on loop conformations. There is a helix dipole interaction with the Zn site, and 14 residues form two or more structurally conserved side-chain to main-chain hydrogen bonds that appear critical to active-site architecture, loop conformation, and the increased stability resulting from the Cys-111----Ser mutation.

PMID: 1463506 [PubMed - indexed for MEDLINE]

PMCID: PMC49447

Structures reported by this article