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DC Field | Value | Language |
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dc.contributor.author | Trinh, Chi H. | - |
dc.contributor.author | Hunter, Therese | - |
dc.contributor.author | Stewart, Emma E. | - |
dc.contributor.author | Phillips, Simon E. V. | - |
dc.contributor.author | Hunter, Gary J. | - |
dc.date.accessioned | 2024-04-11T14:20:28Z | - |
dc.date.available | 2024-04-11T14:20:28Z | - |
dc.date.issued | 2008 | - |
dc.identifier.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. | en_GB |
dc.identifier.uri | https://www.um.edu.mt/library/oar/handle/123456789/120710 | - |
dc.description.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. | en_GB |
dc.language.iso | en | en_GB |
dc.publisher | Wiley-Blackwell Publishing, Inc. | en_GB |
dc.rights | info:eu-repo/semantics/restrictedAccess | en_GB |
dc.subject | Amino acid sequence | en_GB |
dc.subject | Caenorhabditis elegans | en_GB |
dc.subject | Enzymology | en_GB |
dc.subject | Crystallography | en_GB |
dc.subject | Molecules -- Models | en_GB |
dc.subject | Proteins -- Conformation | en_GB |
dc.subject | Superoxide dismutase | en_GB |
dc.title | Purification, crystallization and X-ray structures of two manganese superoxide dismutase from Caernohabditis elegans | en_GB |
dc.type | article | en_GB |
dc.rights.holder | The copyright of this work belongs to the author(s)/publisher. The rights of this work are as defined by the appropriate Copyright Legislation or as modified by any successive legislation. Users may access this work and can make use of the information contained in accordance with the Copyright Legislation provided that the author must be properly acknowledged. Further distribution or reproduction in any format is prohibited without the prior permission of the copyright holder | en_GB |
dc.description.reviewed | peer-reviewed | en_GB |
dc.identifier.doi | 10.1107/S1744309108037056 | - |
dc.publication.title | Acta Crystallographica Section F: Structural Biology and Crystallization Communications | en_GB |
Appears in Collections: | Scholarly Works - FacM&SPB |
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