Download MendeleyStructures of PmSOD1 and PmSOD2, two superoxide dismutases from the protozoan parasite Perkinsus marinus
Asojo, O.A., Schott, E.J., Vasta, G.R., Silva, A.M.(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 1072-1075
- PubMed: 17077482
- DOI: https://doi.org/10.1107/S1744309106040425
- Primary Citation of Related Structures:
2CW2, 2CW3 - PubMed Abstract:
Perkinsus marinus, a facultative intracellular parasite of the eastern oyster Crassostrea virginica, is responsible for mass mortalities of oyster populations. P. marinus trophozoites survive and proliferate within oyster hemocytes, invading most tissues and fluids, thus causing a systemic infection that eventually kills the host. The phagocytosis of P. marinus trophozoites lacks a respiratory burst, suggesting that the parasite has mechanisms that actively abrogate the host's oxidative defense responses. One mechanism and the first line of defense against oxidative damage is the dismutation of superoxide radical to molecular oxygen and hydrogen peroxide by superoxide dismutases (SODs). P. marinus possesses two iron-cofactored SODs, PmSOD1 and PmSOD2. Here, the crystallization and X-ray structures of both PmSOD1 and PmSOD2 are presented.
Organizational Affiliation:
Pathology and Microbiology Department, University of Nebraska Medical Center, 986495 Nebraska Med Center, Omaha, NE 68198-6495, USA. oasojo@unmc.edu
