Prostaglandin H synthase: Implications for membrane structure

Abstract

The crystal structure of the membrane protein prostaglandin H synthase (PGHS) provides strong evidence for the existence of monotopic membrane proteins: PGHS seems to interact with the membrane via a motif of amphipathic helices positioned parallel to the plane of the membrane. The orientation of this unique membrane binding motif is fixed in space by an epidermial growth factor(EGF)‐like module on its amino‐terminal end and by the catalytic domain at its carboxy‐terminal end. The catalytic domain of PGHS has a high structural homology to other mammalian heme peroxidases.