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4qwt

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Revision as of 20:47, 5 August 2016

Anaerobic crystal structure of delta413-417:GS LOX in complex with arachidonate

Structural highlights

4qwt is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Related:	3fgi, 2fnq, 3fg3, 3fg4
Activity:	Arachidonate 8-lipoxygenase, with EC number 1.13.11.40
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AOSL_PLEHO] Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide.^[1] ^[2]

Publication Abstract from PubMed

Lipoxygenases (LOX) play critical roles in mammalian biology in the generation of potent lipid mediators of the inflammatory response; consequently they are targets for the development of isoform-specific inhibitors. The regio- and stereo-specificity of the oxygenation of polyunsaturated fatty acids by the enzymes is understood in terms of the chemistry, but structural observation of the enzyme-substrate interactions is lacking. Although several LOX crystal structures are available, heretofore the rapid oxygenation of bound substrate has precluded capture of the enzyme-substrate complex, leaving a gap between chemical and structural insights. In this report we describe the 2.0 A resolution structure of 8R-LOX in complex with arachidonic acid (AA) obtained under anaerobic conditions. Subtle rearrangements, primarily in the side chains of three amino acids, allow binding of AA in a catalytically competent conformation. Accompanying experimental work supports a model in which both substrate tethering and cavity depth contribute to positioning the appropriate carbon at the catalytic machinery.

Crystal Structure of a Lipoxygenase in Complex with Substrate: the Arachidonic Acid Binding Site of 8R-Lipoxygenase.,Neau DB, Bender G, Boeglin WE, Bartlett SG, Brash AR, Newcomer ME J Biol Chem. 2014 Sep 17. pii: jbc.M114.599662. PMID:25231982^[3]

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

References

↑ Koljak R, Boutaud O, Shieh BH, Samel N, Brash AR. Identification of a naturally occurring peroxidase-lipoxygenase fusion protein. Science. 1997 Sep 26;277(5334):1994-6. PMID:9302294
↑ Boutaud O, Brash AR. Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla. J Biol Chem. 1999 Nov 19;274(47):33764-70. PMID:10559269
↑ Neau DB, Bender G, Boeglin WE, Bartlett SG, Brash AR, Newcomer ME. Crystal Structure of a Lipoxygenase in Complex with Substrate: the Arachidonic Acid Binding Site of 8R-Lipoxygenase. J Biol Chem. 2014 Sep 17. pii: jbc.M114.599662. PMID:25231982 doi:http://dx.doi.org/10.1074/jbc.M114.599662

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qwt"

@@ Line 1: / Line 1: @@
 ==Anaerobic crystal structure of delta413-417:GS LOX in complex with arachidonate==
 <StructureSection load='4qwt' size='340' side='right' caption='[[4qwt]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fgi|3fgi]], [[2fnq|2fnq]], [[3fg3|3fg3]], [[3fg4|3fg4]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arachidonate_8-lipoxygenase Arachidonate 8-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.40 1.13.11.40] </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=4qwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qwt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qwt RCSB], [http://www.ebi.ac.uk/pdbsum/4qwt 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=4qwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qwt OCA], [http://pdbe.org/4qwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qwt RCSB], [http://www.ebi.ac.uk/pdbsum/4qwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qwt ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4qwt" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4qwt

From Proteopedia

Revision as of 20:47, 5 August 2016

Anaerobic crystal structure of delta413-417:GS LOX in complex with arachidonate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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