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    Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6109-13.

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

    Parge HE, Hallewell RA, Tainer JA.

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

    Erratum in

    • Proc Natl Acad Sci U S A 1992 Nov 15;89(22):11106.

    Abstract

    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
    Free PMC Article

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