3DC5

Crystal Structure of a manganese superoxide dismutases from Caenorhabditis elegans

Summary for 3DC5

• Entry DOI: 10.2210/pdb3dc5/pdb
• Related: 3DC6
• Descriptor: Superoxide dismutase [Mn] 2, MANGANESE (II) ION, MALONATE ION, ... (4 entities in total)
• Functional Keywords: alpha hairpin n domain, alpha/beta c domain, oxidoreductase, manganese, metal-binding, mitochondrion, transit peptide
• Biological source: Caenorhabditis elegans (nematode)
• Cellular location: Mitochondrion matrix: P41977
• Total number of polymer chains: 2
• Total formula weight: 44930.88

Authors

Trinh, C.H.,Hunter, T.,Stewart, E.E.,Phillips, S.E.V.,Hunter, G.J. (deposition date: 2008-06-03, release date: 2009-06-09, Last modification date: 2023-11-01)

Primary citation

Trinh, C.H.,Hunter, T.,Stewart, E.E.,Phillips, S.E.,Hunter, G.J.
Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans
Acta Crystallogr.,Sect.F, 64:1110-1114, 2008

PubMed Abstract: 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.

PubMed: 19052361
DOI: 10.1107/S1744309108037056

Experimental method

X-RAY DIFFRACTION (1.7 Å)