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1gp4

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[[Image:1gp4.jpg|left|200px]]
 
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{{Structure
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==Anthocyanidin synthase from Arabidopsis thaliana (selenomethionine substituted)==
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|PDB= 1gp4 |SIZE=350|CAPTION= <scene name='initialview01'>1gp4</scene>, resolution 2.1&Aring;
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<StructureSection load='1gp4' size='340' side='right'caption='[[1gp4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE= <scene name='pdbsite=IRN:2og+Binding+Site'>IRN</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=AKG:2-OXYGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1gp4]] 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=1GP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GP4 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.1&#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=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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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=1gp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp4 OCA], [https://pdbe.org/1gp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1gp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gp4 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gp4 OCA], [http://www.ebi.ac.uk/pdbsum/1gp4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gp4 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/LDOX_ARATH LDOX_ARATH] Involved in anthocyanin and protoanthocyanidin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins. Possesses low flavonol synthase activity in vitro towards dihydrokaempferol and dihydroquercetin producing kaempferol and quercitin, respectively.<ref>PMID:12940955</ref> <ref>PMID:16153644</ref> <ref>PMID:19433090</ref> <ref>PMID:21683773</ref> <ref>PMID:16106293</ref>
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== Evolutionary Conservation ==
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'''ANTHOCYANIDIN SYNTHASE FROM ARABIDOPSIS THALIANA (SELENOMETHIONINE SUBSTITUTED)'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/1gp4_consurf.spt"</scriptWhenChecked>
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Flavonoids are common colorants in plants and have long-established biomedicinal properties. Anthocyanidin synthase (ANS), a 2-oxoglutarate iron-dependent oxygenase, catalyzes the penultimate step in the biosynthesis of the anthocyanin class of flavonoids. The crystal structure of ANS reveals a multicomponent active site containing metal, cosubstrate, and two molecules of a substrate analog (dihydroquercetin). An additional structure obtained after 30 min exposure to dioxygen is consistent with the oxidation of the dihydroquercetin to quercetin and the concomitant decarboxylation of 2-oxoglutarate to succinate. Together with in vitro studies, the crystal structures suggest a mechanism for ANS-catalyzed anthocyanidin formation from the natural leucoanthocyanidin substrates involving stereoselective C-3 hydroxylation. The structure of ANS provides a template for the ubiquitous family of plant nonhaem oxygenases for future engineering and inhibition studies.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1GP4 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=1GP4 OCA].
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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=1gp4 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Structure and mechanism of anthocyanidin synthase from Arabidopsis thaliana., Wilmouth RC, Turnbull JJ, Welford RW, Clifton IJ, Prescott AG, Schofield CJ, Structure. 2002 Jan;10(1):93-103. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11796114 11796114]
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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: Clifton, I J.]]
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[[Category: Clifton IJ]]
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[[Category: Prescott, A G.]]
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[[Category: Prescott AG]]
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[[Category: Schofield, C J.]]
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[[Category: Schofield CJ]]
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[[Category: Turnbull, J J.]]
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[[Category: Turnbull JJ]]
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[[Category: Welford, R W.D.]]
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[[Category: Welford RWD]]
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[[Category: Wilmouth, R C.]]
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[[Category: Wilmouth RC]]
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[[Category: 2-oxoglutarate dependent dioxygenase]]
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[[Category: flavonoid biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:34 2008''
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Current revision

Anthocyanidin synthase from Arabidopsis thaliana (selenomethionine substituted)

PDB ID 1gp4

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