1N0J

The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles

Replaces:  1ABM

Summary for 1N0J

• Entry DOI: 10.2210/pdb1n0j/pdb
• Descriptor: Superoxide dismutase [Mn], MANGANESE (II) ION (3 entities in total)
• Functional Keywords: four-helix bundle, metalloenzyme, manganese, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix: P04179
• Total number of polymer chains: 2
• Total formula weight: 44838.49

Authors

Borgstahl, G.E.O.,Parge, H.E.,Tainer, J.A. (deposition date: 2002-10-14, release date: 2002-11-06, Last modification date: 2024-02-14)

Primary citation

Borgstahl, G.E.,Parge, H.E.,Hickey, M.J.,Beyer Jr., W.F.,Hallewell, R.A.,Tainer, J.A.
The Structure of Human Mitochondrial Mn3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles
Cell(Cambridge,Mass.), 71:107-107, 1992

PubMed 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.

PubMed: 1394426
DOI: 10.1016/0092-8674(92)90270-M

Experimental method

X-RAY DIFFRACTION (2.2 Å)