2ayl

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spinqualitylabelsall models 2ayl, resolution 2.000Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

2AYL is a Single protein structure of sequence from Ovis aries with BOG, FLP, MNH and GOL as ligands. Active as Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1 Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Wed Nov 21 08:27:52 2007