Prostaglandin H synthase: implications for membrane structure.
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 epidermal 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.
Picot
D
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Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.
Garavito
R M
RM
D000595:Amino Acid Sequence; D003460:Crystallization; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011451:Prostaglandin-Endoperoxide Synthases / Q000737:chemistry*; D017433:Protein Structure, Secondary
D046911:Macromolecular Substances; D008565:Membrane Proteins; D011451:Prostaglandin-Endoperoxide Synthases