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PDBsum entry 1prh
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Oxidoreductase(dioxygenase, peroxidase)
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PDB id
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1prh
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The X-Ray crystal structure of the membrane protein prostaglandin h2 synthase-1.
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Authors
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D.Picot,
P.J.Loll,
R.M.Garavito.
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Ref.
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Nature, 1994,
367,
243-249.
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PubMed id
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Abstract
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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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Secondary reference #1
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Title
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X-Ray crystal structure of canine myeloperoxidase at 3 a resolution.
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Authors
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J.Zeng,
R.E.Fenna.
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Ref.
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J Mol Biol, 1992,
226,
185-207.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. Stereo photograph showing te averaged electron density ma on the proximal side of the heme. Residues
R333, Y334 G335, H336, T337, L338 and 1339 are located in helix H8 and include histidine 336, which provides the
proximal ligand to the heme iron. The carboxl group of glutamate 242 can be .seen to occupy electron density that is
continuous-with that of the heme macrocycle
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Figure 4.
Figure 4. tereo photograph of the averaged electon density map corresponding to the first 2 N-acetylglucosamine
(NAG) residues attached to Asn317. The orientations f both sugar molecules are clearly defined by density
corresponding to the N-acetyl groups. From the C5 position of the 1st sugr, electron density (not shown) corresponding
to t,he l-6 linked fucose projcts backwards.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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