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The structure of human mitochondrial manganese superoxide-dismutase reveals a novel tetrameric interface of 2 4-helix bundles

Academic Article
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Overview

authors

  • Borgstahl, G. E. O.
  • Parge, H. E.
  • Hickey, M. J.
  • Beyer, W. F.
  • Hallewell, R. A.
  • Tainer, John

publication date

  • October 1992

journal

  • Cell  Journal

abstract

  • The 2.2 A resolution crystal structure of recombinant human manganese superoxide dismutase, a homotetrameric enzyme that protects mitochondria against oxygen-mediated free radical damage, has been determined. Within each subunit, both the N-terminal helical hairpin and C-terminal alpha/beta domains contribute ligands to the catalytic manganese site. Two identical 4-helix bundles, symmetrically assembled from the N-terminal helical hairpins, form novel tetrameric interfaces that stabilize the active sites. Structurally altered polymorphic variants with reduced activity, such as tetrameric interface mutant Ile-58 to Thr, may produce not only an early selective advantage, through enhanced cytotoxicity of tumor necrosis factor for virus-infected cells, but also detrimental effects from increased mitochondrial oxidative damage, contributing to degenerative conditions, including diabetes, aging, and Parkinson's and Alzheimer's diseases.

subject areas

  • Amino Acid Sequence
  • Gene Library
  • Humans
  • Mitochondria
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Superoxide Dismutase
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/0092-8674(92)90270-m

PubMed ID

  • 1394426
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Additional Document Info

start page

  • 107

end page

  • 118

volume

  • 71

issue

  • 1

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