4hhs: Difference between revisions
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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]] 1.70Å' scene=''> | <StructureSection load='4hhs' size='340' side='right' caption='[[4hhs]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hhs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4hhs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. 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> | ||
</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='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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hhr|4hhr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hhr|4hhr]]</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 | <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 ARATH])</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> | <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://pdbe.org/4hhs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hhs RCSB], [http://www.ebi.ac.uk/pdbsum/4hhs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hhs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4hhs" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arath]] | ||
[[Category: Goulah, C C]] | [[Category: Goulah, C C]] | ||
[[Category: Koszelak-Rosenblum, M]] | [[Category: Koszelak-Rosenblum, M]] | ||
Revision as of 21:55, 5 August 2016
Crystal Structure of fatty acid alpha-dioxygenase (Arabidopsis thaliana)Crystal Structure of fatty acid alpha-dioxygenase (Arabidopsis thaliana)
Structural highlights
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] Publication Abstract from PubMedalpha-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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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