2brj

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[[Image:2brj.gif|left|200px]]
 
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{{Structure
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==X-ray structure of the Allene Oxide Cyclase from Arabidopsis thaliana==
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|PDB= 2brj |SIZE=350|CAPTION= <scene name='initialview01'>2brj</scene>, resolution 1.50&Aring;
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<StructureSection load='2brj' size='340' side='right'caption='[[2brj]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[2brj]] is a 3 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=2BRJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BRJ FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Allene-oxide_cyclase Allene-oxide cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.6 5.3.99.6]
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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]] 1.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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}}
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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=2brj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2brj OCA], [https://pdbe.org/2brj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2brj RCSB], [https://www.ebi.ac.uk/pdbsum/2brj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2brj ProSAT]</span></td></tr>
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</table>
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'''X-RAY STRUCTURE OF THE ALLENE OXIDE CYCLASE FROM ARABIDOPSIS THALIANA'''
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== Function ==
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[https://www.uniprot.org/uniprot/AOC2_ARATH AOC2_ARATH] Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid.
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== Evolutionary Conservation ==
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==Overview==
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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/br/2brj_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=2brj 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 ==
We describe the crystallization and structure elucidation of Arabidopsis thaliana allene oxide cyclase 2 (AOC2), a key enzyme in the biosynthesis of jasmonates. In a coupled reaction with allene oxide synthase, AOC2 releases the first cyclic and biologically active metabolite, 12-oxo-phytodienoic acid (OPDA). AOC2 (AT3G25770) folds into an eight-stranded antiparallel beta-barrel with a C-terminal partial helical extension. The protein forms a hydrophobic binding cavity with two distinct polar patches. AOC2 is trimeric in crystals, in vitro and in planta. Based on the observed folding pattern, we assigned AOC2 as a low molecular weight member of the lipocalin family with enzymatic activity in plants. We determined the binding position of the competitive inhibitor vernolic acid (a substrate analog) in the binding pocket. Based on models for bound substrate 12,13-epoxy-9,11,15-octadecatrienoic acid and product OPDA, we propose a reaction scheme that explains the influence of the C15 double bond on reactivity. Reaction is promoted by anchimeric assistance through a conserved Glu residue. The transition state with a pentadienyl carbocation and an oxyanion is stabilized by a strongly bound water molecule and favorable pi-pi interactions with aromatic residues in the cavity. Stereoselectivity results from steric restrictions to the necessary substrate isomerizations imposed by the protein.
We describe the crystallization and structure elucidation of Arabidopsis thaliana allene oxide cyclase 2 (AOC2), a key enzyme in the biosynthesis of jasmonates. In a coupled reaction with allene oxide synthase, AOC2 releases the first cyclic and biologically active metabolite, 12-oxo-phytodienoic acid (OPDA). AOC2 (AT3G25770) folds into an eight-stranded antiparallel beta-barrel with a C-terminal partial helical extension. The protein forms a hydrophobic binding cavity with two distinct polar patches. AOC2 is trimeric in crystals, in vitro and in planta. Based on the observed folding pattern, we assigned AOC2 as a low molecular weight member of the lipocalin family with enzymatic activity in plants. We determined the binding position of the competitive inhibitor vernolic acid (a substrate analog) in the binding pocket. Based on models for bound substrate 12,13-epoxy-9,11,15-octadecatrienoic acid and product OPDA, we propose a reaction scheme that explains the influence of the C15 double bond on reactivity. Reaction is promoted by anchimeric assistance through a conserved Glu residue. The transition state with a pentadienyl carbocation and an oxyanion is stabilized by a strongly bound water molecule and favorable pi-pi interactions with aromatic residues in the cavity. Stereoselectivity results from steric restrictions to the necessary substrate isomerizations imposed by the protein.
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==About this Structure==
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The crystal structure of Arabidopsis thaliana allene oxide cyclase: insights into the oxylipin cyclization reaction.,Hofmann E, Zerbe P, Schaller F Plant Cell. 2006 Nov;18(11):3201-17. Epub 2006 Nov 3. PMID:17085685<ref>PMID:17085685</ref>
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2BRJ is a [[Single protein]] structure of 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=2BRJ OCA].
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==Reference==
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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 crystal structure of Arabidopsis thaliana allene oxide cyclase: insights into the oxylipin cyclization reaction., Hofmann E, Zerbe P, Schaller F, Plant Cell. 2006 Nov;18(11):3201-17. Epub 2006 Nov 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17085685 17085685]
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</div>
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[[Category: Allene-oxide cyclase]]
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<div class="pdbe-citations 2brj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hofmann, E.]]
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[[Category: Hofmann E]]
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[[Category: Schaller, F.]]
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[[Category: Schaller F]]
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[[Category: Zerbe, P.]]
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[[Category: Zerbe P]]
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[[Category: GOL]]
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[[Category: allene oxide cyclase]]
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[[Category: beta barrel]]
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[[Category: cyclase]]
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[[Category: isomerase]]
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[[Category: jasmonate synthesis]]
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[[Category: transit peptide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:43 2008''
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Current revision

X-ray structure of the Allene Oxide Cyclase from Arabidopsis thaliana

PDB ID 2brj

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