Crystal structure of Cu/Zn superoxide dismutase from Taeniasolium reveals metal-mediated self-assembly

Taeniasolium is the cestode responsible for porcine and human cysticercosis. The ability of this parasite to establish itself in the host is related to its evasion of the immune response and its antioxidant defence system. The latter includes enzymes such as cytosolic Cu/Zn superoxide dismutase. In...

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Bibliographic Details
Published in:The FEBS journal 2011-09, Vol.278 (18), p.3308
Main Authors: Hernández-Santoyo, Alejandra, Landa, Abraham, González-Mondragón, Edith, Pedraza-Escalona, Martha, Parra-Unda, Ricardo, Rodríguez-Romero, Adela
Format: Article
Language:English
Subjects:
Crystal structure
Enzymes
Molecular biology
Parasites
Proteins
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Summary:Taeniasolium is the cestode responsible for porcine and human cysticercosis. The ability of this parasite to establish itself in the host is related to its evasion of the immune response and its antioxidant defence system. The latter includes enzymes such as cytosolic Cu/Zn superoxide dismutase. In this article, we describe the crystal structure of a recombinant T.solium Cu/Zn superoxide dismutase, representing the first structure of a protein from this organism. This enzyme shows a different charge distribution at the entrance of the active channel when compared with human Cu/Zn superoxide dismutase, giving it interesting properties that may allow the design of specific inhibitors against this cestode. The overall topology is similar to other superoxide dismutase structures; however, there are several His and Glu residues on the surface of the protein that coordinate metal ions both intra- and intermolecularly. Interestingly, one of these ions, located on the β2strand, establishes a metal-mediated intermolecular β-β interaction, including a symmetry-related molecule. The factors responsible for the abnormal protein-protein interactions that lead to oligomerization are still unknown; however, high metal levels have been implicated in these phenomena, but exactly how they are involved remains unclear. The present results suggest that this structure could be useful as a model to explain an alternative mechanism of protein aggregation commonly observed in insoluble fibrillar deposits. Database The atomic coordinates and structure factors have been deposited in the Protein Data Bank under the accession number . Structured digital abstract * to by (View Interaction,) * to by * to by (View Interaction,) * to by The crystal structure of a recombinant Taenia solium Cu/Zn superoxide dismutase presents different properties when compared with the human enzyme, which could allow the design of specific inhibitors against this cestode. The T.solium enzyme has several histidine and glutamic acid residues on its surface that coordinate metal ions, one of them establishes metal-mediated intermolecular β/β interaction including symmetry-related molecules. [PUBLICATION ABSTRACT]
ISSN:1742-464X
1742-4658
DOI:10.1111/j.1742-4658.2011.08247.x