Abstract
Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed 0 with glutathione at 2.3 Å resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site which is never seen among other members of the GST family. The unique 3-D architecture of the catalytic cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific conversion of PGH2 to PGD2.
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