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

Borgstahl, Gloria E.O.; Parge, Hans E.; Hickey, Michael J.; Beyer, Wayne F.; Hallewell, Robert A.; Tainer, John A.

doi:10.1016/0092-8674(92)90270-m

Cited by 472Enzyme Structure and FunctionMetal-Catalyzed Oxygenation MechanismsProtein Structure and Dynamics

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

Borgstahl, Gloria E.O., Parge, Hans E., Hickey, Michael J., Beyer, Wayne F., Hallewell, Robert A., Tainer, John A.·1992·Cell

DOI 10.1016/0092-8674(92)90270-m

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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.

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The active sites and structures of three MnSODs (human, Escherichia coli, and Deinococcus radiodurans) have been studied in detail.
“The active sites and structures of three MnSODs (human, Escherichia coli, and Deinococcus radiodurans) have been studied in detail [80,81,82].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [80]

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Authors: Borgstahl, G. E. O., Parge, H. E., Hickey, M. J., Beyer, W. F., Hallewell, R. A., & Tainer, J. A.
Affiliations: Scripps Research Institute (US)
Duke University (US)
ORCID: Tainer, John A.
Venue: Cell
Publisher: Elsevier BV
Published: 1992-10
Volume: 71
Issue: 1
Pages: 107-118
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/0092-8674(92)90270-m
OpenAlex: W2093212227
Cited by: 472
References: 89
Citations by year: 2026: 9 · 2025: 10 · 2024: 18 · 2023: 13 · 2022: 11 · 2021: 17 · 2020: 9 · 2019: 15 · 2018: 21 · 2017: 19 · 2016: 15 · 2015: 12 · 2014: 26 · 2013: 17 · 2012: 16
FWCI: 5.64
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM-39345, R01GM039345)
Topics: Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: manganese superoxide dismutase, four-helix bundle, homotetramer, crystal structure, alpha/beta domain, polymorphic variants, mitochondrial oxidative damage, Parkinson's disease, Alzheimer's disease, diabetes mellitus, aging
MeSH terms: Amino Acid Sequence, Humans, Mitochondria, Models, Molecular, Molecular Sequence Data, Protein Conformation, Recombinant Proteins, Superoxide Dismutase, X-Ray Diffraction, Gene Library, Protein Structure, Secondary, Protein Structure, Tertiary

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

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