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Nature. 1994 Jan 20;367(6460):243-9.

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

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1
Department of Biochemistry and Molecular Biology, University of Chicago, Illinois 60637.

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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PMID:
8121489
DOI:
10.1038/367243a0
[Indexed for MEDLINE]
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