This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2ayl

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 13:37, 10 September 2015

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

Structural highlights

2ayl is a 2 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Related:	1q4g, 1eqh, 1eqg, 1ht5, 1ht8, 1prh
Activity:	Prostaglandin-endoperoxide synthase, with EC number 1.14.99.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PGH1_SHEEP] May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

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

References

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ayl"

@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q4g|1q4g]], [[1eqh|1eqh]], [[1eqg|1eqg]], [[1ht5|1ht5]], [[1ht8|1ht8]], [[1prh|1prh]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prostaglandin-endoperoxide_synthase Prostaglandin-endoperoxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.99.1 1.14.99.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ayl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ayl RCSB], [http://www.ebi.ac.uk/pdbsum/2ayl PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ayl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayl OCA], [http://pdbe.org/2ayl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ayl RCSB], [http://www.ebi.ac.uk/pdbsum/2ayl PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ayl" style="background-color:#fffaf0;"></div>
 ==See Also==

2ayl

From Proteopedia

Revision as of 13:37, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox