3fg3

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[[Image:3fg3.png|left|200px]]
 
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==Crystal structure of Delta413-417:GS I805W LOX==
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The line below this paragraph, containing "STRUCTURE_3fg3", creates the "Structure Box" on the page.
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<StructureSection load='3fg3' size='340' side='right'caption='[[3fg3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fg3]] 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=3FG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FG3 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</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>
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{{STRUCTURE_3fg3| PDB=3fg3 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg3 OCA], [https://pdbe.org/3fg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fg3 RCSB], [https://www.ebi.ac.uk/pdbsum/3fg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fg3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/3fg3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fg3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Lipoxygenases (LOX) play pivotal roles in the biosynthesis of leukotrienes and other biologically active eicosanoids derived from arachidonic acid. A mechanistic understanding of substrate recognition, when lipoxygenases that recognize the same substrate generate different products, can be used to help guide the design of enzyme-specific inhibitors. We report here the 1.85 A resolution structure of an 8R-lipoxygenase from Plexaura homomalla, an enzyme with a sequence approximately 40% identical to that of human 5-LOX. The structure reveals a U-shaped channel, defined by invariant amino acids, that would allow substrate access to the catalytic iron. We demonstrate that mutations within the channel significantly impact enzyme activity and propose a novel model for substrate binding potentially applicable to other members of this enzyme family.
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===Crystal structure of Delta413-417:GS I805W LOX===
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The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity.,Neau DB, Gilbert NC, Bartlett SG, Boeglin W, Brash AR, Newcomer ME Biochemistry. 2009 Aug 25;48(33):7906-15. PMID:19594169<ref>PMID:19594169</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19594169}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3fg3" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19594169 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19594169}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3fg3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FG3 OCA].
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==Reference==
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<ref group="xtra">PMID:19594169</ref><ref group="xtra">PMID:18007054</ref><references group="xtra"/>
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[[Category: Arachidonate 8-lipoxygenase]]
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[[Category: Plexaura homomalla]]
[[Category: Plexaura homomalla]]
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[[Category: Neau, D B.]]
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[[Category: Neau DB]]
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[[Category: Newcomer, M E.]]
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[[Category: Newcomer ME]]
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[[Category: Arichidonic metabolism]]
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[[Category: Calcium]]
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[[Category: Cytoplasm]]
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[[Category: Dioxygenase]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Heme]]
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[[Category: Iron]]
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[[Category: Lipid synthesis]]
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[[Category: Lipoxygenase]]
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[[Category: Lyase]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Multifunctional enzyme]]
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[[Category: Oxidoreductase]]
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[[Category: Oxylipin biosynthesis]]
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Current revision

Crystal structure of Delta413-417:GS I805W LOX

PDB ID 3fg3

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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