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Title: | Purification, crystallization and X-ray structures of two manganese superoxide dismutase from Caernohabditis elegans |
Authors: | Trinh, Chi H. Hunter, Therese Stewart, Emma E. Phillips, Simon E. V. Hunter, Gary J. |
Keywords: | Amino acid sequence Caenorhabditis elegans Enzymology Crystallography Molecules -- Models Proteins -- Conformation Superoxide dismutase |
Issue Date: | 2008 |
Publisher: | Wiley-Blackwell Publishing, Inc. |
Citation: | Trinh, C. H., Hunter, T., Stewart, E. E., Phillips, S. E., & Hunter, G. J. (2008). Purification, crystallization and X-ray structures of the two manganese superoxide dismutases from Caenorhabditis elegans. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(12), 1110-1114. |
Abstract: | Caenorhabditis elegans expresses two manganese superoxide dismutase enzymes (MnSOD-2 andMnSOD-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 P41212 for each, with unit-cell parameters a = b = 81.0, c = 137.4 A ° forMnSOD-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 Rfree = 26.2% at 293 K, and R = 18.9% and Rfree = 22.6% at 100 K, while that of MnSOD-2 was refined to R = 16.9% and Rfree = 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. |
URI: | https://www.um.edu.mt/library/oar/handle/123456789/120710 |
Appears in Collections: | Scholarly Works - FacM&SPB |
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