PDBsum entry 3dc5

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Oxidoreductase PDB id
Protein chains
194 a.a.
_MN ×2
Waters ×420

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Key reference
Title Purification, Crystallization and X-Ray structures of the two manganese superoxide dismutases from caenorhabditis elegans.
Authors C.H.Trinh, T.Hunter, E.E.Stewart, S.E.Phillips, G.J.Hunter.
Ref. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008, 64, 1110-1114.
PubMed id 19052361
Caenorhabditis elegans expresses two manganese superoxide dismutase enzymes (MnSOD-2 and MnSOD-3) that are targeted to the mitochondrion. MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible. The structures of these two mononuclear metalloenzymes have been determined to 1.8 and 1.7 A resolution, respectively. Pink crystals formed in space group P4(1)2(1)2 for each, with unit-cell parameters a = b = 81.0, c = 137.4 A for MnSOD-2 and a = b = 81.8, c = 136.0 A for MnSOD-3. The final structure of MnSOD-3 was refined to R = 21.6% and R(free) = 26.2% at 293 K, and R = 18.9% and R(free) = 22.6% at 100 K, while that of MnSOD-2 was refined to R = 16.9% and R(free) = 20.1% at 100 K. The asymmetric unit cell is comprised of two subunits. The resulting structures are very similar to that of human MnSOD and form a tetramer corresponding to a dimer of dimers. The subunit interface between dimers is comprised of two four-helix bundles that stabilize the biologically significant homotetramer.
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