1n0j
From Proteopedia
|
The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles
Overview
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.
About this Structure
1N0J is a Single protein structure of sequence from Homo sapiens with MN as ligand. This structure superseeds the now removed PDB entry 1ABM. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
Reference
The structure of human mitochondrial manganese superoxide dismutase reveals a novel tetrameric interface of two 4-helix bundles., Borgstahl GE, Parge HE, Hickey MJ, Beyer WF Jr, Hallewell RA, Tainer JA, Cell. 1992 Oct 2;71(1):107-18. PMID:1394426
Page seeded by OCA on Mon Nov 12 18:16:24 2007
