1PRH

THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 SYNTHASE-1

Summary for 1PRH

• Entry DOI: 10.2210/pdb1prh/pdb
• Descriptor: PROSTAGLANDIN H2 SYNTHASE-1, PROTOPORPHYRIN IX CONTAINING FE (2 entities in total)
• Functional Keywords: oxidoreductase(dioxygenase, peroxidase)
• Biological source: Ovis aries (sheep)
• Cellular location: Endoplasmic reticulum membrane; Multi-pass membrane protein: P05979
• Total number of polymer chains: 2
• Total formula weight: 128967.66

Authors

Picot, D.,Loll, P.J.,Garavito, R.M. (deposition date: 1994-03-07, release date: 1995-03-31, Last modification date: 2024-10-23)

Primary citation

Picot, D.,Loll, P.J.,Garavito, R.M.
The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1.
Nature, 367:243-249, 1994

PubMed Abstract: The three-dimensional structure of prostaglandin H2 synthase-1, an integral membrane protein, has been determined at 3.5 A resolution by X-ray crystallography. This bifunctional enzyme comprises three independent folding units: an epidermal growth factor domain, a membrane-binding motif and an enzymatic domain. Two adjacent but spatially distinct active sites were found for its haem-dependent peroxidase and cyclooxygenase activities. The cyclooxygenase active site is created by a long, hydrophobic channel that is the site of non-steroidal anti-inflammatory drug binding. The conformation of the membrane-binding motif strongly suggests that the enzyme integrates into only one leaflet of the lipid bilayer and is thus a monotopic membrane protein.

PubMed: 8121489
DOI: 10.1038/367243a0

Experimental method

X-RAY DIFFRACTION (3.5 Å)