1PRH

The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1.

(1994) Nature 367: 243-249

• PubMed: 8121489 Search on PubMed
• DOI: https://doi.org/10.1038/367243a0
• Primary Citation of Related Structures:  
  1CQE, 1PRH


• 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.

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Organizational Affiliation: 

Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.