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[[Image: | ==Crystal structure of Delta413-417:GS I805A LOX== | ||
<StructureSection load='3fg4' size='340' side='right' caption='[[3fg4]], [[Resolution|resolution]] 2.31Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3fg4]] 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=3FG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACD:ARACHIDONIC+ACID'>ACD</scene>, <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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fnq|2fnq]], [[3fg1|3fg1]], [[3fg3|3fg3]]</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=3fg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fg4 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg4 PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/3fg4_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Arachidonate 8-lipoxygenase]] | [[Category: Arachidonate 8-lipoxygenase]] | ||
[[Category: Plexaura homomalla]] | [[Category: Plexaura homomalla]] | ||
[[Category: Neau, D B | [[Category: Neau, D B]] | ||
[[Category: Newcomer, M E | [[Category: Newcomer, M E]] | ||
[[Category: Arichidonic metabolism]] | [[Category: Arichidonic metabolism]] | ||
[[Category: Dioxygenase]] | [[Category: Dioxygenase]] | ||
Revision as of 11:45, 26 November 2014
Crystal structure of Delta413-417:GS I805A LOXCrystal structure of Delta413-417:GS I805A LOX
Structural highlights
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 PubMedLipoxygenases (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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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