View source for 4qwt


==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=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qwt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QWT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.002&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACD:ARACHIDONIC+ACID'>ACD</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qwt OCA], [https://pdbe.org/4qwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qwt RCSB], [https://www.ebi.ac.uk/pdbsum/4qwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qwt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AOSL_PLEHO 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.<ref>PMID:9302294</ref> <ref>PMID:10559269</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25231982</ref>

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/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Plexaura homomalla]]
[[Category: Neau DB]]
[[Category: Newcomer ME]]