1w07

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{{Seed}}
 
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[[Image:1w07.png|left|200px]]
 
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==Arabidopsis thaliana acyl-CoA oxidase 1==
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The line below this paragraph, containing "STRUCTURE_1w07", creates the "Structure Box" on the page.
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<StructureSection load='1w07' size='340' side='right'caption='[[1w07]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1w07]] is a 2 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=1W07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W07 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr>
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{{STRUCTURE_1w07| PDB=1w07 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w07 OCA], [https://pdbe.org/1w07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w07 RCSB], [https://www.ebi.ac.uk/pdbsum/1w07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w07 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACOX1_ARATH ACOX1_ARATH] Catalyzes the desaturation of both long- and medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Most active with C14-CoA. Activity on long-chain mono-unsaturated substrates is 40% higher than with the corresponding saturated substrates. Seems to be an important factor in the general metabolism of root tips. May be involved in the biosynthesis of jasmonic acid.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w0/1w07_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1w07 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The peroxisomal acyl-CoA oxidase family plays an essential role in lipid metabolism by catalyzing the conversion of acyl-CoA into trans-2-enoyl-CoA during fatty acid beta-oxidation. Here, we report the X-ray structure of the FAD-containing Arabidopsis thaliana acyl-CoA oxidase 1 (ACX1), the first three-dimensional structure of a plant acyl-CoA oxidase. Like other acyl-CoA oxidases, the enzyme is a dimer and it has a fold resembling that of mammalian acyl-CoA oxidase. A comparative analysis including mammalian acyl-CoA oxidase and the related tetrameric mitochondrial acyl-CoA dehydrogenases reveals a substrate-binding architecture that explains the observed preference for long-chained, mono-unsaturated substrates in ACX1. Two anions are found at the ACX1 dimer interface and for the first time the presence of a disulfide bridge in a peroxisomal protein has been observed. The functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments.
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===ARABIDOPSIS THALIANA ACYL-COA OXIDASE 1===
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Acyl-CoA oxidase 1 from Arabidopsis thaliana. Structure of a key enzyme in plant lipid metabolism.,Pedersen L, Henriksen A J Mol Biol. 2005 Jan 21;345(3):487-500. PMID:15581893<ref>PMID:15581893</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_15581893}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1w07" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15581893 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15581893}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1W07 is a 2 chains structure of sequences 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=1W07 OCA].
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==Reference==
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<ref group="xtra">PMID:15581893</ref><references group="xtra"/>
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[[Category: Acyl-CoA oxidase]]
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Henriksen, A.]]
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[[Category: Large Structures]]
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[[Category: Pedersen, L.]]
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[[Category: Henriksen A]]
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[[Category: Fad cofactor]]
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[[Category: Pedersen L]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxisomal beta-oxidation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:30:10 2009''
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Current revision

Arabidopsis thaliana acyl-CoA oxidase 1

PDB ID 1w07

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