2CW3

X-ray structure of PmSOD2, superoxide dismutase from Perkinsus marinus

Summary for 2CW3

• Entry DOI: 10.2210/pdb2cw3/pdb
• Related: 2cw2
• Descriptor: iron superoxide dismutase, FE (III) ION (3 entities in total)
• Functional Keywords: sod, oxidoreductase
• Biological source: Perkinsus marinus
• Total number of polymer chains: 2
• Total formula weight: 63428.19

Authors

Asojo, O.A.,Schott, E.J.,Vasta, G.R.,Silva, A.M. (deposition date: 2005-06-16, release date: 2006-07-04, Last modification date: 2024-03-13)

Primary citation

Asojo, O.A.,Schott, E.J.,Vasta, G.R.,Silva, A.M.
Structures of PmSOD1 and PmSOD2, two superoxide dismutases from the protozoan parasite Perkinsus marinus
ACTA CRYSTALLOGR.,SECT.F, 62:1072-1075, 2006

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.

PubMed: 17077482
DOI: 10.1107/S1744309106040425

Experimental method

X-RAY DIFFRACTION (2.5 Å)