The crystal structure of seleno-glutathione peroxidase from human plasma at 2.9 A resolution

Journal of Molecular Biology
B RenR Ladenstein

Abstract

Glutathione peroxidase belongs to the family of selenoproteins and plays an important role in the defense mechanisms of mammals, birds and fish against oxidative damage by catalyzing the reduction of a variety of hydroperoxides, using glutathione as the reducing substrate. However, the physiological role of human plasma glutathione peroxidase remains unclear due to the low levels of reduced glutathione in human plasma and the low reactivity of this enzyme. The crystal structure of human plasma glutathione peroxidase was determined by Patterson search methods using a polyalanine model modified from the known structure of bovine erythrocyte glutathione peroxidase. The structure was refined to a crystallographic R-factor of 0.228 (R(free) = 0.335) with I > 2sigma(I) reflections in the resolution range of 8 to 2.9 A. The asymmetric unit contains a dimer. Tetramers are built up from dimers by crystallographic symmetry. The subunit structure of the plasma enzyme shows the typical structure motif of the thioredoxin fold consisting of a central beta-sheet and several flanking alpha-helices. The active site selenocysteine residue is situated in the loop between beta1 and alpha1 and is located in a pocket on the protein surface. The over...Continue Reading

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