2ayl

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2ayl, resolution 2.00Å ()
Ligands: , , , , ,
Activity: Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1
Related: 1q4g, 1eqh, 1eqg, 1ht5, 1ht8, 1prh
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

2.0 Angstrom Crystal Structure of Manganese Protoporphyrin IX-reconstituted Ovine Prostaglandin H2 Synthase-1 Complexed With Flurbiprofen

Publication Abstract from PubMed

Prostaglandin H2 synthase (EC 1.14.99.1) is a clinically important drug target that catalyzes two key steps in the biosynthesis of the eicosanoid hormones. The enzyme contains spatially distinct cyclooxygenase and peroxidase active sites, both of which require a heme cofactor. Substitution of ferric heme by Mn(III) protoporphyrin IX greatly diminishes the peroxidase activity, but has little effect on the cyclooxygenase activity. Here, the 2.0 angstroms resolution crystal structure of the Mn(III) form of ovine prostaglandin H2 synthase-1 is described (R = 21.8%, R(free) = 23.7%). Substitution of Mn(III) for Fe(III) causes no structural perturbations in the protein. However, the out-of-plane displacement of the manganese ion with respect to the porphyrin is greater than that of the iron by approximately 0.2 angstroms. This perturbation may help to explain the altered catalytic properties of the manganese enzyme.

2.0 angstroms structure of prostaglandin H2 synthase-1 reconstituted with a manganese porphyrin cofactor., Gupta K, Selinsky BS, Loll PJ, Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):151-6. Epub 2006, Jan 18. PMID:16421446

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2ayl is a 2 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA.

See Also

Reference

  • Gupta K, Selinsky BS, Loll PJ. 2.0 angstroms structure of prostaglandin H2 synthase-1 reconstituted with a manganese porphyrin cofactor. Acta Crystallogr D Biol Crystallogr. 2006 Feb;62(Pt 2):151-6. Epub 2006, Jan 18. PMID:16421446 doi:10.1107/S0907444905036309

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