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==Crystal Structure of fatty acid alpha-dioxygenase (Arabidopsis thaliana)==
==Crystal Structure of fatty acid alpha-dioxygenase (Arabidopsis thaliana)==
<StructureSection load='4hhs' size='340' side='right' caption='[[4hhs]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='4hhs' size='340' side='right'caption='[[4hhs]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4hhs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HHS FirstGlance]. <br>
<table><tr><td colspan='2'>[[4hhs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HHS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hhr|4hhr]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">T13O15.6, alphaDOX1, At3g01420/T13O15.6, DOX1, At3g01420, AT3G01420 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</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=4hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhs OCA], [https://pdbe.org/4hhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hhs RCSB], [https://www.ebi.ac.uk/pdbsum/4hhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhs 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=4hhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hhs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hhs RCSB], [http://www.ebi.ac.uk/pdbsum/4hhs PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DOX1_ARATH DOX1_ARATH]] Alpha-dioxygenase that catalyzes the primary oxygenation of fatty acids into oxylipins. Mediates a protection against oxidative stress and cell death, probably by generating some lipid-derived molecules. Promotes local and systemic plant defense in a salicylic acid (SA)-dependent manner, including the establishment of systemic acquired resistance (SAR) in response to incompatible interaction. Involved in a negative regulation of abscisic acid (ABA)-mediated signaling pathway.<ref>PMID:12060227</ref> <ref>PMID:10455113</ref> <ref>PMID:22199234</ref> 
[https://www.uniprot.org/uniprot/DOX1_ARATH DOX1_ARATH] Alpha-dioxygenase that catalyzes the primary oxygenation of fatty acids into oxylipins. Mediates a protection against oxidative stress and cell death, probably by generating some lipid-derived molecules. Promotes local and systemic plant defense in a salicylic acid (SA)-dependent manner, including the establishment of systemic acquired resistance (SAR) in response to incompatible interaction. Involved in a negative regulation of abscisic acid (ABA)-mediated signaling pathway.<ref>PMID:12060227</ref> <ref>PMID:10455113</ref> <ref>PMID:22199234</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Dioxygenases (alpha-DOX) oxygenate fatty acids into 2(R)-hydroperoxides. Despite the low level of sequence identity, alpha-DOX share common catalytic features with cyclooxygenases (COX), including the use of a tyrosyl radical during catalysis. We determined the X-ray crystal structure of Arabidopsis thaliana alpha-DOX to 1.5 A resolution. The alpha-DOX structure is monomeric, predominantly alpha-helical, and comprised of two domains. The base domain exhibits a low degree of structural homology with the membrane-binding domain of COX but lies in a similar position with respect to the catalytic domain. The catalytic domain shows the highest degree of similarity with the COX catalytic domain, where 21 of the 22 alpha-helical elements are conserved. Helices H2, H6, H8, and H17 form the heme binding cleft and walls of the active site channel. His-318, Thr-323, and Arg-566 are located near the catalytic tyrosine, Tyr-386, at the apex of the channel, where they interact with a chloride ion. Substitutions at these positions coupled with kinetic analyses confirm previous hypotheses that implicate these residues as being involved in binding and orienting the carboxylate group of the fatty acid for optimal catalysis. Unique to alpha-DOX is the presence of two extended inserts on the surface of the enzyme that restrict access to the distal face of the heme, providing an explanation for the observed reduced peroxidase activity of the enzyme. The alpha-DOX structure represents the first member of the alpha-DOX subfamily to be structurally characterized within the cyclooxygenase-peroxidase family of heme-containing proteins.
 
The Crystal Structure of alpha-Dioxygenase Provides Insight into Diversity in the Cyclooxygenase-Peroxidase Superfamily.,Goulah CC, Zhu G, Koszelak-Rosenblum M, Malkowski MG Biochemistry. 2013 Feb 14. PMID:23373518<ref>PMID:23373518</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Goulah, C C]]
[[Category: Large Structures]]
[[Category: Koszelak-Rosenblum, M]]
[[Category: Goulah CC]]
[[Category: Malkowski, M G]]
[[Category: Koszelak-Rosenblum M]]
[[Category: Zhu, G]]
[[Category: Malkowski MG]]
[[Category: Calcium binding]]
[[Category: Zhu G]]
[[Category: Cyclooxygenase myeloperoxidase folding]]
[[Category: Fatty acid dioxygenase]]
[[Category: Monotopic membrane protein]]
[[Category: Oxidoreductase]]

Latest revision as of 14:41, 1 March 2024

Crystal Structure of fatty acid alpha-dioxygenase (Arabidopsis thaliana)Crystal Structure of fatty acid alpha-dioxygenase (Arabidopsis thaliana)

Structural highlights

4hhs is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DOX1_ARATH Alpha-dioxygenase that catalyzes the primary oxygenation of fatty acids into oxylipins. Mediates a protection against oxidative stress and cell death, probably by generating some lipid-derived molecules. Promotes local and systemic plant defense in a salicylic acid (SA)-dependent manner, including the establishment of systemic acquired resistance (SAR) in response to incompatible interaction. Involved in a negative regulation of abscisic acid (ABA)-mediated signaling pathway.[1] [2] [3]

References

  1. ↑ De Leon IP, Sanz A, Hamberg M, Castresana C. Involvement of the Arabidopsis alpha-DOX1 fatty acid dioxygenase in protection against oxidative stress and cell death. Plant J. 2002 Jan;29(1):61-2. PMID:12060227
  2. ↑ Hamberg M, Sanz A, Castresana C. alpha-oxidation of fatty acids in higher plants. Identification of a pathogen-inducible oxygenase (piox) as an alpha-dioxygenase and biosynthesis of 2-hydroperoxylinolenic acid. J Biol Chem. 1999 Aug 27;274(35):24503-13. PMID:10455113
  3. ↑ Vicente J, Cascon T, Vicedo B, Garcia-Agustin P, Hamberg M, Castresana C. Role of 9-lipoxygenase and alpha-dioxygenase oxylipin pathways as modulators of local and systemic defense. Mol Plant. 2012 Jul;5(4):914-28. doi: 10.1093/mp/ssr105. Epub 2011 Dec 22. PMID:22199234 doi:10.1093/mp/ssr105

4hhs, resolution 1.70Å

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