3fg3: Difference between revisions

Revision as of 22:06, 7 February 2016

Crystal structure of Delta413-417:GS I805W LOX

Structural highlights

3fg3 is a 4 chain structure with sequence from Black sea rod. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ACY, CA, CL, FE2, GOL
Related:	2fnq, 3fg1, 3fg4
Activity:	Arachidonate 8-lipoxygenase, with EC number 1.13.11.40
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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]

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

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^[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, Gilbert NC, Bartlett SG, Boeglin W, Brash AR, Newcomer ME. The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity. Biochemistry. 2009 Aug 25;48(33):7906-15. PMID:19594169 doi:10.1021/bi900084m

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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

[2] 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

[3] Neau DB, Gilbert NC, Bartlett SG, Boeglin W, Brash AR, Newcomer ME. The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity. Biochemistry. 2009 Aug 25;48(33):7906-15. PMID:19594169 doi:10.1021/bi900084m

[1]

[2]

[3]

@@ Line 2: / Line 2: @@
 <StructureSection load='3fg3' size='340' side='right' caption='[[3fg3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fg3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_sea_rod Black sea rod]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FG3 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]], [[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=3fg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fg3 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg3 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=3fg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fg3 OCA], [http://pdbe.org/3fg3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3fg3 RCSB], [http://www.ebi.ac.uk/pdbsum/3fg3 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
      <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].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ 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 3fg3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 33: / Line 34: @@
 </StructureSection>
 [[Category: Arachidonate 8-lipoxygenase]]
-[[Category: Plexaura homomalla]]
+[[Category: Black sea rod]]
 [[Category: Neau, D B]]
 [[Category: Newcomer, M E]]

3fg3: Difference between revisions

Revision as of 22:06, 7 February 2016

Crystal structure of Delta413-417:GS I805W LOX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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