2fnq: Difference between revisions

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<StructureSection load='2fnq' size='340' side='right'caption='[[2fnq]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='2fnq' size='340' side='right'caption='[[2fnq]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fnq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_sea_rod Black sea rod]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zq4 1zq4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FNQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fnq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plexaura_homomalla Plexaura homomalla]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zq4 1zq4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FNQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1u5u|1u5u]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2fnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fnq OCA], [https://pdbe.org/2fnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fnq RCSB], [https://www.ebi.ac.uk/pdbsum/2fnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fnq ProSAT]</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=2fnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fnq OCA], [http://pdbe.org/2fnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fnq RCSB], [http://www.ebi.ac.uk/pdbsum/2fnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fnq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>
[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>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=2fnq 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=2fnq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lipoxygenases (LOXs) catalyze the regio- and stereospecific dioxygenation of polyunsaturated membrane-embedded fatty acids. We report here the 3.2 A resolution structure of 8R-LOX from the Caribbean sea whip coral Plexaura homomalla, a LOX isozyme with calcium dependence and the uncommon R chiral stereospecificity. Structural and spectroscopic analyses demonstrated calcium binding in a C2-like membrane-binding domain, illuminating the function of similar amino acids in calcium-activated mammalian 5-LOX, the key enzyme in the pathway to the pro-inflammatory leukotrienes. Mutation of Ca(2+)-ligating amino acids in 8R-LOX resulted not only in a diminished capacity to bind membranes, as monitored by fluorescence resonance energy transfer, but also in an associated loss of Ca(2+)-regulated enzyme activity. Moreover, a structural basis for R chiral specificity is also revealed; creation of a small oxygen pocket next to Gly(428) (Ala in all S-LOX isozymes) promoted C-8 oxygenation with R chirality on the activated fatty acid substrate.
Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality.,Oldham ML, Brash AR, Newcomer ME J Biol Chem. 2005 Nov 25;280(47):39545-52. Epub 2005 Sep 14. PMID:16162493<ref>PMID:16162493</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fnq" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arachidonate 8-lipoxygenase]]
[[Category: Black sea rod]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Brash, A R]]
[[Category: Plexaura homomalla]]
[[Category: Newcomer, M E]]
[[Category: Brash AR]]
[[Category: Oldham, M L]]
[[Category: Newcomer ME]]
[[Category: Beta-barrel]]
[[Category: Oldham ML]]
[[Category: C2-like domain]]
[[Category: Eicosanoid]]
[[Category: Fatty acid]]
[[Category: Oxidoreductase]]

Latest revision as of 12:24, 14 February 2024

Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chiralityInsights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chirality

Structural highlights

2fnq is a 2 chain structure with sequence from Plexaura homomalla. This structure supersedes the now removed PDB entry 1zq4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:,
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  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

2fnq, resolution 3.20Å

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