PDBsum entry 2cw2

Oxidoreductase

PDB id: 2cw2

Contents

Protein chains

199 a.a.

Metals

_FE ×2

Waters ×409

References listed in PDB file

Key reference

• Title: Structures of pmsod1 and pmsod2, Two superoxide dismutases from the protozoan parasite perkinsus marinus.
• Authors: O.A.Asojo, E.J.Schott, G.R.Vasta, A.M.Silva.
• Ref.: Acta Crystallograph Sect F Struct Biol Cryst Commun, 2006, 62, 1072-1075. [DOI no: 10.1107/S1744309106040425]
• PubMed id: 17077482

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.

Figure 1.
Figure 1 (a) Ribbon diagram of the PmSOD1 dimer showing Fe ions (purple spheres) at the active sites with their ligands. At the center of the figure, Glu165 interacts across the dimer interface with the metal ligand His166. (b) Close-up of the active site of PmSOD1 shows the Fe ion (represented as a large yellow sphere) coordinated by three histidine residues, an aspartic acid residue and a water molecule. The water molecule, whose O-atom location is represented as a small red sphere, is coordinated by Gln76.

The above figure is reprinted by permission from the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 1072-1075) copyright 2006.